1) AlP: a-naphthyl phosphate 10 mg, diazo blue B 20 mg Clark and Lub's buffer ph 9.2 2) AcP: a-naphthyl phosphate 10 mg, diazo 3) 0-Est: 0-naphthyl acetate 10 mg, diazo blue B 20 mg, Michaelis buffer Malic dehydrogenase (MDH), a-glycerophosphate dehydrogenase (a-gdh), Glutamic dehydrogenase (GDH),G-Hydrogybutyric dehydrogenase (f3-hdh), Glucose-6-phate dehydrogenase 5) kc1 l 6-bromo-2-naphthyl-ƒÀ-d-glucuronide blue B 20 mg, Michaelis buffer ph 5.8 20 ml ph 7.2 20 ml nase (SDH), Lactic dehydrogenase (LDH), 4) AmP: 1-leucyl-$-naphthylamine hydrochroride 8 mg, acetate buffer ph 6.5 10 mg, 2/100 M KCN 1 ml, diazo blue B 10 mg 37 C, 30 `60 15mg, phosphocitric buffer ph 4.95 10 ml, me- CID D 0.02 M hposphate buffer ph 7.5 50 cc, diazo blue B 50 mg. 1) SDH: M/5 sodium succinate 5 ml, M/10 phosphate buffer ph 7.6 5 ml, nitro BT 5 mg/3 ml 6 ml, Aq, dest. 10 ml, 2) I,DH : M/2 sodium lactate 4 ml, M/10 phosphate buffer ph 7.5 10 ml, nitro BT 5 mg/ 3 ml 3m1, 100% NAD 2,5 ml, M/2 HC1 5 drops 3) MDH: 1M sodium malate 5 ml, M/10 phosphate buffer ph 7,4 10 ml, nitro BN 5 mg/3
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4) Oka, R., et al., Histochemical evaluation of alkaline and acid phosphatase activities in oral neoplastic tissues, J. Osaka Univ. Dent. School, 2 : 25-32, 1962. 5) Cohen, R.B., et al.: Histochemical demonstration of esterase in malignant tumors, Cancer Res., 11 : 709-711, 1951. 6) Braun-Falco, 0.: Histochemische Aminopeptidase Darstellung in normaler Haut bei Psoriasis, Dermatitis, Basaliom, spinozellula- Karzinom und Molluscum sebaseum, ren Dermat. Wchnshr., 134 : 1341-1349, 1956. 8) Okamoto, Y., et al.: Histochemical study of aminopeptidase in neoplasms and inflammatory tissues, J. Osaka Univ. Dent. School, 1 : 53-65, 1961. 9) Glenner, G.G., et al.: A study of aminope- ptidase activity in the stroma of neoplastic tisue with a comparison of histochemical techniques, J. Nat. Cancer Inst., 23 : 857 873, 1959. 10) Monis, B., et al.: Study of leucine aminopeptidase in neoplastic and inflammatory tissues with a new histochemical method, Cancer, 12 : 601-608,1959. 11) Fishman, W.H., and Bigelow, D.R.: A comparative study of the morphology and glu- curonidase activity in 44 gastrointestinal neoplasms, J. Nat. Cancer Inst., 10 : 1115-1122, 1950. 12) Monis, B., et al.: 13-Glucuronidase activity in malignant neoplasms of man; A histochemical study, Cancer, 13 : 386-393,1960. 13) Mori, M., et al.: Histochemical observations of succinic, Malic and Lactic dehydrogenases in oral tumors, Oral Surg., Oral Med., and Oral Path., 17 : 352-363,1964. 14) Monis, B., et al.: Histochemical study of 3 dehydrogenase systems in human tumors, Cancer, 12 : 1238-1247, 1959. 16) Pearse, A.E., Expansion of the limits of cellular pathology; The roll of enzyme histo- chemistry, J. Clin. Path., 11 : 520-534, 1958. 2) Kawakatu, K., and Mori, M., Histochemical 17) Mori, M., et al.: Histochemical study on evaluation of enzymatic activities in human the localization of glucose-6-phosphate dehydrogenase in human tumors, Gann, 54 433 squamous cell cancer, Cancer Res., 23 : 539 545, 1963. - 442, 1963. - 3) Monis, B., et al.: Alkaline phosphatase activity in neoplastic and inflammatory tissues localization of isocitric dehydrogenase in hu- 18) Mori, et al.: Histochemical studies on the of man, Cancer, 13 : 538-544, 1960. man tumors, Gann, 55 : 117-123, 1964.
Abstract Five cases of esophageal carcinoma, two of esophageal leukoplakia and one of carcinoma of tongue were investigated enzyme-histochemically. Enzymes studied in the study were alkaline phosphatase, acid phosphatase, Ĉ-esterase, aminopeptidase and Ĉ-glocuronidase as hydrolytic enzymes, and succinic dehydrogenase, lactic dehydrogenase, malic dehydrogenase, a-glycerophosphate dehydrogenase glutamic dehydrogenase, Ĉhydroxybutyric dehydrogenase, glucose-6-phosphate dehydrogenase and isocitric dehydrogenase as oxidative enzymes. The activity of alkaline phosphatase and aminopeptidase were negative in squamous cell carcinoma, but occasionally positive in stromal element, especially in that of infiltrating carcinoma. Succinic dehydrogenase activity of normal esophageal epithelium was stronger in basal cell layer than in keratinized layer. Other NAD dependent enzymes of it showed a similar tendency. On the other hand the activity of NADP dependent glucose-6-phosphate dehydrogenase of it was stronger in keratinized layer than in basal cell layer. Generally, these squamous cell carcinomas appeared weak enzyme activity, but glucose- 6-phosphate dehydrogenase activity was rather stronger than other enzymes. Some infiltrating marginal area and small cell nestle of carcinomas showed rather strong activities of succinic, Ĉ-hydoxybutyric and malic dehydrogenases, also pearl formation revealed moderate activity of glucose-6-phosphate dehydrogenase. Enzymatic activity in stromal element of all cases was very weak.