Nagamatsu Y, Yamamoto J, Kanamoto A, Tsuda Y, Okada Y
Faculty of Nutrition, Kobe-Gakuin University, Japan.
Chem Pharm Bull (Tokyo). 1992 Jun;40(6):1634-6. doi: 10.1248/cpb.40.1634.
Poly-L-lysine with molecular masses of 3.3-290 kDa increased the amidolytic activities of leukocyte elastase and cathepsin G at low concentration, but had little effect on the activities of pancreatic elastase, alpha-chymotrypsin, plasmin and thrombin. Highly purified cathepsin G was obtained from column of EAH Sepharose 4B or Suc-L-Tyr-D-Leu-D-Val-pNA-Sepharose (affinity chromatography) by elution with poly-L-lysine solution (0.4 mg/ml, molecular weight (MW.) 290000 or 2.2 mg/ml, MW. 3300). Leukocyte elastase, adsorbed to Suc-L-Tyr-D-Leu-D-Val-pNA-Sepharose, was not eluted with poly-L-lysine solution. The amino acid composition of purified cathepsin G has been determined.
分子量为3.3 - 290 kDa的聚-L-赖氨酸在低浓度时可提高白细胞弹性蛋白酶和组织蛋白酶G的酰胺水解活性，但对胰腺弹性蛋白酶、α-糜蛋白酶、纤溶酶和凝血酶的活性影响很小。通过用聚-L-赖氨酸溶液（0.4 mg/ml，分子量（MW.）290000或2.2 mg/ml，MW. 3300）洗脱，从EAH Sepharose 4B柱或Suc-L-Tyr-D-Leu-D-Val-pNA-Sepharose（亲和色谱）中获得了高度纯化的组织蛋白酶G。吸附到Suc-L-Tyr-D-Leu-D-Val-pNA-Sepharose上的白细胞弹性蛋白酶不能用聚-L-赖氨酸溶液洗脱。已测定了纯化的组织蛋白酶G的氨基酸组成。
