HISTOLOGY OF AND CYTOCHEMISTRY PHOSIHORYLASE RICHARD Arnold Biological Although it is very 4, A. ELLIS few, except have attempt Japanese this of the tlsis appems(lages technique outer root arrectores sheath pilorum, of of fornss ansylose side tise molecule of glycogen. for short stmuin By of the presence glucosidase tissues present in or in tissues that Ims tlsis relative conseentratiomss of skin paper, mire glycogems used normally biopsy ins these unsatisfactory. * This 2l25(C7), the with foumnd AND specimens stuidies; end evidence of amyloshould 1 , 6be States the as ml. aultopsy types of Public Health were excised. frozens They can iO ml. MIS acetate controls were ulsed. In one, the solution (5 ml. water) native glycogen which the amybose never solution, the stains type observed Lugol’s for red. (staining in U.S.P., demonstriution blue either of Polysaccharides of with the iodine) control sec- imsctihating 120 minutes, and put into a large volume of dilute Lugol’s iodine solution and gently agitated for 2 to 3 minutes at room temperature. The sections were then were after 2, floated removed 5, 10, onto from 20, clean 40, thie 60, slides the in The colors fade for weeks intense after several when the 90, and glycerine jelly, containing a few trated Lugol’s solution. The sites activity appear blue-black; those plums amylo-1,6-glucosidase are (10). mounted with drops of concenof phospisorybase of phosphorylase reddisis brown. days; slides and are they remain stored in the refrigerator. OBSEniVATIONS skin were sole, palm, Two kinds of reaction products are synsthiesized in the cells when sections of skin mire inscuihated with gluncose-i-phosphate. One group of these RG- consists specimens supported of age, were water, distilled Sections distribution normal of human 67 years they distilled METHODS was investigation and enzymes there of Specimens United these tneatus, axilla, mutsd otiser of the body of nude mind 10 to as soon 95 ml. media boealization of compsured MATERIALS Only and emszymes Island tions. tlsat normally store glycogen normally utilize glycogen or tissues arnylose. humami their 15 were demonstrable is indirect of plsosphiorylase activity. Tlsese subjects ice of tissues can be iodine. histoebsensically minimal in since auditory regions in dry Lungol’s polysaccharide withs Rhode 19, 1957 female Two syn- incubating fresh tisese enzymes 12, sections were placed into the incubating solution without the substrate , glucose1 -phosphate , mind in the other, they were placed directly insto dilumte branch- enzymes branchsed, differently presence Tlse glycogen the polymers to form * buffer at pH 4.8, i5 units of insulin, and 5 mg. of glycogen maintained at 37#{176}C. The newer met hod containing 20% alcohol by volume (12) offered no improvement in the localization of the enszymes. ,6-glucosidase these simubtamseoumsbv products to ehaimi msecessary of time, ilensonstrated the catnu1 -phsos- linked Amylo-1 large, periods and l)ecember acid, thus Together, thesize follicles straight type. chains. in common of the Abomse , phosphorylase limskages between glucose 1 , 6 linkages tlse ing rich skin of exception are producing the example, amylo1 , 6-glueosidase reaction glucoseand the cutaneous generally the the SITES be stored frozen from a few hours to two dmuvs without diminishing enzyme activity. Skins from the backs and soles of cats, guiinea pigs, rabbits, rats, and mice were used for comparison. Fresh frozen sections, 15 to 70 jz in thiickmsess, were removed from the blade of the microtome and placed directly into the incumbating medium of Takeuchi and Kuriaki (15); this consists of 50 mg. glucose-i-phosphate, 10 mg. muscle adenybic of in For of active hsair have nomse. glycogenesis. only 1 ,4 molecules, aware other are its with gbycogen, ;: process cai form be who occur 16). nsost skims Pisosphorylase and lyze the reversible phsate (2, human those animals, laboratory must and (16, Those that enzyme in )hospliorylase, enzyme. differences epidermis (15), XV. ACTIVITY Providence scalp, external representative localize investigators this species presemsee whiile the use great to SKIN. MONTAGNA University, for publication easy HUMAN 6-GLEJCOSIDASE , WILLIAM AND Brown histochemically studied to the relrutively activity 14), AMYLO-1 Laboratory, Received phosphorylase OF AND were by of Service. the of amylose short, straight type 201 Downloaded from jhc.sagepub.com by guest on February 4, 2015 and chain stnuins pobysaccharides a h)lue-green or 202 RICHARD bluse-black color the branched barge, glycogen, (13). formed stains The from iodine; blune-staining by or combinsed action AND consists of stratum of enzymatic which the is by and the Tmucheuchi (1 ) have sumcceeded glumcosidmuse inhibited not is nione the The enzyme is for incubating is nsuch more in and control some tion of these mige, we The enzymes is different Normal stratuns spinosuim stratumnss cormseumns epidermis phosphsorylase, both emszynses, seems ins the paIns ans(l with isas the append- epidermis stratum the strmutum both of be basabe stratums only the An the the stratum sole and in both stratuns glycogen forms in as hosphorylase hasale. Skin housr the the spinosum. In the then, before be demonstrate in the require stratum up to periods useful a little an strong enzymatic longer particumlarly only after and any visualized; not to- children, spinosum incubation are of minutes, is present aged may can phosphorypresent skin activity from the of sole in the mis 2 reac- and accumulated stratum short the are In of spinosuim, mask palm palm, layers. of formatioms they is tund incunbation incubating and the minumtes, spinosumm, amylo-1,6-glucosidase activity; more of because phosphorylase In contain is activity (Fig. eccrine of Eccrine dermis, (1) (2) a coiled glands secretory and a coil straight the nial, spiral “sweat duct unit.” The coiled secrecoil contains more phosphorybase than ansy structure in the skin. The coiled and the tory other strmuight some rich in enzyme, but parts activity in can be The In the within in the mihove part of it dumct are dumct spiral spinous the secretory (3) amm intraepider- also the epidermis, straight of the the tise towards the connect and sweat a of the duct that with the epidermis, are present glands: segments: part ment thick i). sweat three the enzymatic enzymes may spinosum The consist (leel) in the subject. while the are gether has detected. granubosum of and some 10 in glycogen basale to that After give After results in spino- sections stratumm intenssely no stratum pobysaccharide. basale. longer minutes, stratum they different any scant enzymes of most epidermis camsnot 20 5 the stratumss glycogen. incubation and in reactive the the activity. age devoid thins and sole each phosphorylase is weakly or time in different is Ins very absesst localiza- aduilt of amylo-1 , 6-glucosidnuse, regions, and varying The strat tins basabe either the for in so reaction activ- and some in comstains the of control for compousnds for either type cobor or stain one contain 1, 6-glucosidase conscentrations activity. pres- emich separately. epidermis: modermute the neither the incubation which amybo-1,6-glunco- of activity described sec- tissues, indicating amybo- in mind seems of it in sections in lase abuindant appendages degree glucose-i- unimscubated cutaneouts the me- epidermis forms epidermis sidase. Since which tion with incubation, phosphorylase or spinosuns occasionally traces iodine amylose lost of and ity. and nsinumtes periods etsce of 1)0th phosphorylase Most is 40 houmr of incubation synthesized before five and ,6- is apparently authors. it is in the than mint! amybo-1 contmiminsated. gbycogen tions ing and to these periods phosphate, tissues (10), ansybose Braun-Fabco enzyme two iodinse be short This by i)y nsust After nor (letisOnstrat the utsed (13), phosphsorylase dunrinsg inscumh)ation had in thsmus destrove(i dium ml. its tissimes. labile also et is only imscumbating ansylo-1,6- stratumn adult or glycogen Neither misore Normal, a positive glumcosidase. and activity lucidum. suns produced of phosphorylase basale glycogen phosphor- misahogany-staimsing is MONTAGNA stratum polysaccharide glycogemi, WILLIAM molecumles or mahogany molecumles 1 ,4 bimskages; pOlysiicchari(Ie, ELLIS other a red-brown gluicose joimss the polysaccharide which color ylmise with A. is completely is unreactive in the phosphorybase gradumally epidermal bayer rich seg- sweat reactive, (Fig. decreases. duct humt 1). unit that There Figures 1 to 8 mire mull freshi frozen sections of hummamm skin incumbated at 37#{176}C.in the substrate nsixture of Takeunchi ati(1 Kurimiki (15) for the demonstration of phosphorylase and amylo-1 ,6-glucosidase activit)-. The reactions l)rotlulcts were visualized by staining with dilumte Lugob’s iodine solution. Ftc. 1 . A 40 z sections of l)abmfl from a 48 year old man. The gyres of the eccrine sweat dumct are negative for I)isosphorlase ins the straum corneum, bumt intensely reactive in the stratum spinosumm mind in the dernsis i)elow. Amvlo-1 ,6-glucosidase amid phosphoryliuse ture both present ims the stratum spinosumm of the epidermis. 20 miniumte itscubmition, X 90. Fnc. 2. Pisosphorvlase activity in an eccrine sweat dumct of the abdominal skin of a 53 yemur old womami. The remuction ins the duct is instemsse at the dermab level, diminishing, as it approaches the surfmuce, to the same intemmsitv mis the epidernsis. 40 section incunbated 10 minutes, X 200. FIG. 3. A thick section throumgh a growimig hair fobicle in the external auditory meatuis of a 37 yemir 01(1 man. Both ansylo-1 ,6-glumcosidase and phosphorylase are present in the epidermis. The duct of mimi apocrimse cerumnimioums gland is intensely reactive where it opens into the pibosebaceous canal; the activity vanishes proximal to its secretory segment. Intense enzymatic activity is also present iii the outer root sheath surrounding the hmuir shaft. 20 minumtes incubations, X 90. Fmc. 4. Secret orv coils of apocrine and eccrine a mmmi 52 years old. The eccrinse tumi)tlles (top) (bottom) are nsegative. 40 section incumbated sweat are very 40 minumtes, glands lying side-by-side rich in phosphorylase X 180. Downloaded from jhc.sagepub.com by guest on February 4, 2015 in the axiblary while the apocrine orgams of tumbumles HISTOLOGY - .. .- -. -‘-... AND CYTOCHEMISTRY - OF HUMAN SKIN. IV 203 - . a 1 - p 1 _ .. Fmt;s. 1-4 Downloaded from jhc.sagepub.com by guest on February 4, 2015 204 is RICHARD no evidence in eccrine for during If incumi)ation, Amybose iodine glycogenm it amybose 2 a gen in free thsese show it Thse . cells is reactions time h)einsg rich tion gradumabby decreasing (Fig. activity sweat. dumct stratums tion 2). in to In the dunct eccrine examine(1 (Fig. glands all level in phosphorepidermal bevel superficial unreactive for The apocrine glands sweat of the noums glands in deep in dermis; in the the the pilary the animals The secretory and auditory a short, below or sebaceous above the glands or secretory 4); portion the activity amstl mit its tise activity proaches thse (Inlet the is as eccritse tion peripheral entrance of to swemut of the of or amybo-i duct begins jumnction show the the follicle in (Fig. colors 3). an The instense terminal an intense The ouster quiescent and hair active aroumnd the blue or blume-green color in both phosphorylase stains is bower zone, which contains the The of in the cells of the In contrast with have found matrix cuticle Braun-Falco’s no color intense keratogenoums sheath that particumlarly we por- blue after an of and a reddish very little phosphorybase activity; enzyme in the cells of the upper part of of the half particuslarly native ap- region of the of the ouiter the shows some it umpper phosphorylase, sheath reaction glycogens. iodine In only and this the and most tubumle that to phosphorylase sheath contains in incubated enzyme as terminal as The active root gener- glycogen aroumnd the is the part neither some intensity Both contains iodine; sections negative 10 enzyme native abundant most least appreciable of always outer the at control amylo-i,6-glucosidase, the contain are follicle mictivity activity has secretory canal. The ins phosphorylase glands dumct glands to with increases pilary rich the , 6-glucosidase show The canal. incubated activity. stains iodine. which and 6). pilary cells. have the the the gland and enzymatic of be by in the 5 sebaceous follicle: the of (Figs. amounnts hair with decreases center phos- peripheral demonstrated unincumbated follicles of of strong the already wall to small to in strong the order sections which with Tue (Fig. the half portion activity cells, The contain follicles, of surface. phsosphorylase has in amybo-1,6-glucosidase opens directly sebum must ally hair lies duct the the that in test. The cerummi- meatus straight toward peripheral control coil the The dusct to activity. por- he Neither ansy Moderate localized as (1). minutes phosphorybase organ external canal of the duct glands: axillary gland, in The can tubunbes. iii ,6- incubation, pobysacehsaride glycogen is phosphorybase, activity even thoumgh all of them contain glycogen normally; only those of the cat show a small amotmnt of phosphorylase and amylo-1 , 6-gluncosidase activity in the secretory segment. the the cells similar secrecontain amylo-1 of secretor)- glan(ls: activity sebaceouss enzyme. staining sebaceous of anti periods showed the glmuisds gland. disappears of t.he short the controls sweat phosphorybase blue apocrine mature of the of laboratory the mind Braumn-Fabco the sole, the the no same of red cells reac- present of at 1), containing sweat are or part the concen- 20 to 40 mm- sumrroundling apocrine After sumrroumnding The apical cells the amounts phorybase the the of seen and are unreacbecomes less the abruptly granuilosumm light in is palm spiral stops the surface, thmut the umnit of thse The time muctivity ylase phosphorylase, thse nuclei the duct a)promiches phosphorybase epidermis 1)0th A maximal is mittaine(l after myoepithelial some the 5 minutes. incubation. coils of completely its strong only glyco- sections mire only glumcosidase. di- of of particumbarly it as of amylose small and stained ansoumnt i)umt control cytoplasm portiomss of the cells; tive. Ins thin epidernsis reactive of tration tory with incubating sections sumbstrate equmably MONTAGNA incubation umtes the segment (bumct after mmsmall strumctuires, without of (lark by blue-black secretory of tue Constrol ioditse itscubmite(I mmusked deep ins the portiomss with there WILLIAM The stains minsutes. rectly activity is synthesized is completely is symsthsesized only AND reaction. that in time deeper ELLIS amnybo-1,6-glucosidase glands. intense A. the bulb there bulb is and of the hair. (1) observation, phosphorylase in Humxbey’s layer or in any part of the inner root sheath. Fno. 5. A 40 sei)miceolis cells mmns(1 the sei)umm for pisosphorylase. sectioms through a sebaceoums gland in the scalp of a 57 yemsr old woman. The peripheral constain some phosphorylase and amylo-1,6-glucosidase. bumt the centers of the lobumles mire umnreactive. The arrector pili mumscle below the sebaceotms gland is stromsgly reactive 40 minsumtes incumi)mution, X90. FIG. 6. Phosphorylase and amylo-i ,6-glumcosidase activity in a small sebaceous g’and in the skin of the externmii aumditory meat us of a 37 year old mats. The peripheral cells are remuctive for both enzymes, while time center of the glansd hsmis mulmost mso activity. 30 section incubated 20 minumtes, X 250. Fnu. 7. A sections through two hair follicles in the resting stage. The hair germ (arrow) mmd the oumter root sisemuth of tise hair bulb (above) are rich in phosphorylase, while the cells that form the sheath of the p piloseimceous cotstaits mmnsylo-l ,6-glucosidase in addition. 20 mimsumtes incumbation, lower portions of mu resting hair follicle at a higher magniifications. The catsmil Fto. 8. The bumlb above it imonse of enszyme. the constain ahunmdant 30p sections, phosphorylase, X 320. hut the dermal papilla Downloaded from jhc.sagepub.com by guest on February 4, 2015 (arrow) hair of the X 00. germ hair and the (Iontaimms HISTOLOGY AND CYTOCHEMISTRY OF HUMAN SKIN. 205 IV ..J p .‘ 0 11 ‘0 PLATE Imcs. 2 5-S Downloaded from jhc.sagepub.com by guest on February 4, 2015 200 HICHAIII) In the restinsg hair club follicles hair, contains amid tue the (Figs. reactive The hut the fmurthser the where it canmul, phosphorylase amsd sonsw level al)Sence in of slowing 1)0th constains amybo-i less the the murrcctores piloruins hair smill ,6-glucosidase phosphorylmise activit\ black color with in skins of the tue examisimsed. iodine tisese in tue to immcubate level mumscles sweat 10 to test after for 20 the he considerably mnitsutes to are also cells rich in reactions identifying the of hsummmn technique have activity that Our a positive activity the of be as ins fresh This a means frozen tlse of of thsams skin. Abundant them after tures the in greater the DISCUSSION glycogen, small tlse of cells \Vlsems tbie nsav et basabe two tlse in bmuyer lisns different withs in the both comstains mammals epidermis spinsosuns. glycogens, epi(lernsis of upomi depend way formssation tlsese of the this imscubated amsinsals these enzyme Since have is distinctly us the cornified layer. epidermis not, Thsere man other human is a direct ninsount anti distribution epidernssis antI the height succinic dehydrogemsuuse chensical features tissue. The richly vascularized gland (3). In These striking apocrine These two bution Tlse extent chsildren active amxl the virtual thse amsd already tluet Isas is tiot thse not glands a in hsisto- an active is secretory the rich othser of eccrimse tlse contrast also part as of properties the of withs the eccrine glands glands, in of glycogen. localization certain comscentra- of the comstain a therefore, spite of the follicles of their the enzyme Downloaded from jhc.sagepub.com by guest on February 4, 2015 these state are profoundly superficial struc- distribution activity occasionally only in the (listri- enzymes of sweat no phosphorylase. tural similarity whsich they may exhibit. The presemsce of phosphorylase the duct of apocrimse glands parallels mins(lmunsvlo-1 ,6-glucosidase highs the abumndant length dIuct is also (8) are organs reflects very and entire strengtheuss as hyperreturns structure. glands, different of sweat mictivity glycogen that The se- glycogen. thtrimsg onsce tlse part prob- w-ith characteristic duct quiescent of 5). Tise (7, the enzymes (ieplete(i thesis entity for activity. ams important bound are passive follicles The of are of of all the does (liffereist. tlse enzynses epitiermis that that densonstrated two the studied also nsetabo- systems tise and enzvnses we tioms of phosphorybase in the of Only whems laboratory frons technique. relationship between of and be glamsds the in periods storage Findimsg these is far of demonstrated these restored well-docunsented study basale not ins msearby of be (6), they quickly cells enzymatic are tise Braun- structures longer nsust (11). normal duct Our stratumis and the stratuns the since activity phospisorylase stratuns in stores cretion to basal require secretion function , gland substantial sugars ecerine Braun-Falco spinsosuns. for reducimsg thse gbyeogen amid ansybo- 1, 6-ghmcosidase, in sonse this ably Takeuehi mind differentiates, carbohydrate must in -plsosphsate. the grows of glycogen hasale. in of (10). imsjured essenstial stores glucose-i Sitsce seen often spinosuni ims the tlse readily with are while stratummss enzynsses glvcogen, it epidernsis, phosplsorylmuse tlse free mimvbo-phosphorybase pisosphsorylase 1)0th isormssalbv strmitum phosplsorvlmu.se audI is beems bias us tue Isummums found sisows stratuns even found of (1) of upper el)i(iermis ml. (13) layer ansoumsts tise mup)emur Since epidernsis of amylose), 6-glucositiase. only substrate, of thsis two and one-Isalf while the other struc- for skin of pobysacelsaride other can incubation in the of the sweat amylose frozen comsfirms that the be can fresis demonstration inscubation in is is amylose conditions the abundant mimylo-1 eccrine that in the observation the amylose glands for these whsicls of iso Perhaps shows imscubation color optimal demonstration tlit’ (luring sweat sweat and glycogen because the ageing. Umsder any of timed ) (1 (10) activity. imstemsse skin. series minutes sectionss (:3). Aithiougis glycogets is odd are synthesis the (1). unsed ecerine tubules in Falco’s occurs walls humsian phosphorlmuse (producinsg and less advantageous to necessary is phosphorylase cans arterioles skin .seetioiss obtain ins This we it maximal by reaction. reactive below simsce nsaskedl also in sonse the indicatioms with conditions, its sonsse turmiover plsospisorylase fornsed gives of cell experinsental that mugeti rate demonstrated a blue- enszynsatic glamids, nsusscle charmucteristic are in of 60 to 90 nsimsutes. snsooth arterioles they rich stain animals ansvlose; ams inculi)mition The atsd of mumst eccrine iodinse (1); 5) babormutory The in (Fig. are of the constains intense of abundant mssumscles thsat every glands (Fig. 7). Thse tlse Nearly is of MONTAGNA around sheath forms it WILLIAM phosphorybase root ai)oVe unp, l)ilosel)mmceoums of outer insnsse(liately dumb, below ANI) it sac gems mmnsoumit 7 mmtl(1 8). ELLIS epithelial hair mu mo(lerate A. activity, of its ansd glycogen. is strongest hair to a In mi the HISTOLOGY outer root amsd siseath. Ims tlse lower particularly al)ove aroumsd the 1)0th bulb, tise thse siseath part contains of onsbv sition fromss u.n active lower part of the thse uper l)mtrt retaining geriss by the of :unsvlo-1 In systems thse tran- state, even and intact. The is largely root hair has activity, the 5. some h)ut no , 6-glucosidase. 6. bocalizatioms of 1 , ti-glucosidase surgical sole, axilla, these known epidernsis is the spinsosunni. vmiry with age while A i)umtthe rensmtmnder glands glamsd tory coils, bumt the ins thosphiorylase. i)Oths ims Neither thse comstmiin either duet anti is ricbser in of the skin. but thse emszyme duset Time etszynses, censtrated the mseither of these of the of glands 12. the secretory 13. phosphorylase The in is cells thse activity, apocrine their glands pisosphorylase censters ii. sheaths, glamscls sebaceous periphsermul 10. anti duet enzymatic secreis rich 14. the gland. nor the sehum 15. 16. 1. BRAUN-FALCO, nsenschlichen 0.: Uher Haut zur (lie Fahigkeit Polysaccharidsyn- der the to (Letter anti Cytochem., H.: FANGER, of humman of human (In press). and bioof amybo- . sweat III. Structure Academic 1{educimsg H. Inc. w. C., of phosphorylase. New B. AND distribumtioms W., MONTAGNA, mind Function Press, CHASE, W., B. : The of H. CHASE, York, HAIiIToN, gbycogen skin. J. Inv. I)erm., B. AND and 17: 147LOBITZ, : Histology and cyto-chemistry of hunman skin. II. The distribution of glycogen in the epidermis, hair follicles, sehaceoums glands, anti eccrine sweat glands. Ansmit. Bee., 114: 231-301 , 1952. SHELLEY, W. B., AND MESCON, H.: Histochemicab demonsstrations of secretory activity in humman eccrine sweat glands. J. Iusv. 1)erm., 18: 289-301, 1952. TAKEUCHI, T.: Histochemical demonstration JR. (Letter to the Editor.) J. Histochem. and Cytochem., 4: 84, 1956. TAKEUCHn, T., HIGA5HI, K. AND WATAMUKI, S.: Distribution of amybophosphorylase variouns tissumes of human and mamnsalian organs. J. Histochem. amid Cytochens., TAKEUCHI, in 3: 1955. T., AND demonstration in blood and hone 11: 375-379, 1956. emszvme. REFERENCES W. : “The MONTAGNA, chemical con- of of 1)abmar MONTAGNA, 485-491, contain more and heart. substances (glucose) . Arch. 1)ermat. Syphilol., 56: 819-826, 1947. LoBnTz, W. C., JR., AND MASON, II. I. : Chemistry of palmar sweat. VII. Discuission of stumdies oms chloride, urea, glucose, uric acid, ammonsia nitrogen and creatimsine. Arcis. Dermat. Syphilol., 57:907-915, 1948. lipids in humman 157, 1951. found amvbo- the der 202: phsosphorylase in human embryos. Igakti Kenkvu (Acta Medica), 27: 1659-1688, 1957. L0BITz, W. C., JR., HOLYOKE, H. B. AND BR0PIIY D. : Histochemical evidence for human eccrine sweat duct activity. A.M.A. Arch. 1)ermatol., 72: 229-236. LoBm’rz, W. C., JR., AND OSTERBERG, A. 1.: J. phosphorylase. iso structure lsave only 9. follicles anti of J. Histochem. of Skin.” 1956. enzymes root epidernsal bias of thse thans amsy other sweat isair oumter the glamsds of of the Growing 8. thse stratum epidermis contains of sweat portioms their ones portion amybo- is phsosplsorylase restimsg shsort eccrimse (lomsor. itS which The the the 7. few cells in and of abumidant in phsosphorybase amounts 1, 6-glucosidase other but basale the and present thicknsess of palm, normally. relative thse the hsmuve wlsile in the With variability, stratumss The with found generally spimsosum, 1)0th ili body. glycogen SOIS5C 1 , fi-glucosidase stratum are comstain shsows the amylo- studied from meatus, of enzymes to skin miuditory regions exceptions been hunsan externsmul and bias of representative are pisosphorylase activity specimens Editor.) Histotopocisemie kIm. cxl). Derm., M. : Phosphorylase system Chemistry SUMMARY The L. CARBONELL, 207 IV 3: 419, 1955. :3. EmLms, R. A., MONTAGNA, W. AND Histology and cytochemssistry skin. XIV. The i)iOOd supply cutaneous glands. J. Imsv. Derns., 4. KOBAYAKAWA, S. : Histochemical chemical study on the distribumtions fornsed sheath, pls0sl)isor-bmIse the dlegenerates, whiichs outer 2. root the quieseenst SKIN. condunctive outer mostly follicles, (Iemssomsstrabbe thse unlisturbed emszymsse (PIIS a follicle of quiesceust contains HUMAN these, em Beitrag zur Phosphorylase. Arch. 163-170, 1956. zone , 6-glueosidase. phsosphorylase. to OF follicle, sheath follicle renismuiiiing its of the amy!o-1 tise CYTOCHEMISTRY keratogenous root mind upper part tlse outer phosphorylase Ins AND KmN0SHITA, of marrow cells. K.: Histophosphorylase J. Hemmutol., T., AND KURIAKI, H.: Histochemical detection of phosphorylase in animal tissumes. J. Histochem. and Cytochemis., 3: 153-160, 1955. WATANUKI, S.: Histochemicab distributions of issume amylophosphorylase in various an i mabs. Igakum Kenkyun (Acta Medica), 27: 1059-1128, 1957. 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