Woessner J F
Adv Exp Med Biol. 1977;95:313-27. doi: 10.1007/978-1-4757-0719-9_19.
The purity of cathepsin D has been increased from 150 units/mg to over 200 units/mg. Peptides such as Ala-Phe-NH2, His-Phe-NH2 and Phe-Phe were split by impure enzyme and activity was blocked by pepstatin and diazoacetylnorleucine methyl ester. Pure preparations no longer digested these peptides. This points to the presence of a second peptidase activity similar to cathepsin D in specificity and inhibition properties, but distinct from it . Cathepsin D splits the peptides Leu-Phe-NH2, Leu-Tyr-NH2, Ac-Phe-TyrI2, and Ala-Leu-Tyr-Leu upon overnight incubation. More rapid splitting is found with phenyl sulfite, Glu-Ala-Leu-Tyr-Leu-Val, and Bz-Arg-Gly-Phe-Phe-Leu-4-methoxy-beta-naphthylamide. Digestion of bovine hemoglobin and human serum albumin by ruptured rat liver tritosomes was studied over the pH range 2.5-6.5. The combined action of cathepsin D and thiol proteinases accounted for most of the digestion. Cathepsin D accounted for 75% of the hemoglobin digestion at pH 3 and 45% at pH 5. Thiol proteinase accounted for 85% of the albumin digestion at pH 5. The role of cathepsin D in the development of embryonic limbs and skin, in uterine involution, and in cartilage degradation was reviewed. The activity of cathepsin D on cartilage matrix proteoglycans is limited to acid pH values. Human articular cartilage also contains metalloproteases active at pH 4.5 and 5.7.
组织蛋白酶D的纯度已从150单位/毫克提高到200单位/毫克以上。诸如丙氨酸-苯丙氨酸-氨基、组氨酸-苯丙氨酸-氨基和苯丙氨酸-苯丙氨酸等肽可被不纯的酶裂解，其活性可被胃蛋白酶抑制剂和重氮乙酰正亮氨酸甲酯阻断。纯制剂不再消化这些肽。这表明存在第二种肽酶活性，其在特异性和抑制特性方面与组织蛋白酶D相似，但与之不同。组织蛋白酶D在过夜孵育后可裂解肽亮氨酸-苯丙氨酸-氨基、亮氨酸-酪氨酸-氨基、乙酰基-苯丙氨酸-酪氨酸I2和丙氨酸-亮氨酸-酪氨酸-亮氨酸。用苯基亚硫酸盐、谷氨酸-丙氨酸-亮氨酸-酪氨酸-亮氨酸-缬氨酸和苄基-精氨酸-甘氨酸-苯丙氨酸-苯丙氨酸-亮氨酸-4-甲氧基-β-萘酰胺可实现更快的裂解。研究了在pH 2.5 - 6.5范围内破裂的大鼠肝微粒体对牛血红蛋白和人血清白蛋白的消化作用。组织蛋白酶D和巯基蛋白酶的联合作用占了大部分消化过程。在pH 3时，组织蛋白酶D占血红蛋白消化的75%，在pH 5时占45%。在pH 5时，巯基蛋白酶占白蛋白消化的85%。综述了组织蛋白酶D在胚胎肢体和皮肤发育、子宫复旧以及软骨降解中的作用。组织蛋白酶D对软骨基质蛋白聚糖的活性仅限于酸性pH值。人关节软骨还含有在pH 4.5和5.7时具有活性的金属蛋白酶。
