结缔组织激活。XXXIII. 来自人血小板的CTAP-III的生物活性裂解产物。
Connective tissue activation. XXXIII. Biologically active cleavage products of CTAP-III from human platelets.
作者信息
Castor C W, Walz D A, Ragsdale C G, Hossler P A, Smith E M, Bignall M C, Aaron B P, Mountjoy K
机构信息
Rackham Arthritis Research Unit, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor 49109-0358.
出版信息
Biochem Biophys Res Commun. 1989 Sep 15;163(2):1071-8. doi: 10.1016/0006-291x(89)92330-9.
Evidence for three new isoforms of CTAP-III from human platelets is presented; two NH2-terminal cleavage products were identified, CTAP-III (des 1-13) and CTAP-III (des 1-15). CTAP-III (des 1-13) has a pI of 8.6 and is a relatively stable proteolytic cleavage product that retains the capacity to stimulate [14C]GAG synthesis in human synovial cell cultures. CTAP-III (des 1-15) appears to be an elastase or chymotrypsin cleavage product and identical to NAP-2, an entity thought to have neutrophil activating properties.
本文提供了来自人血小板的三种新的CTAP-III同工型的证据；鉴定出了两种NH2末端裂解产物，即CTAP-III（缺失1-13位氨基酸）和CTAP-III（缺失1-15位氨基酸）。CTAP-III（缺失1-13位氨基酸）的等电点为8.6，是一种相对稳定的蛋白水解裂解产物，保留了刺激人滑膜细胞培养物中[14C]糖胺聚糖合成的能力。CTAP-III（缺失1-15位氨基酸）似乎是一种弹性蛋白酶或胰凝乳蛋白酶裂解产物，与NAP-2相同，NAP-2被认为具有中性粒细胞激活特性。
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