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Purification and characterization of alpha 1-thiol proteinase inhibitor and its identity with kinin- and fragment 1.2-free high molecular weight kininogen.

作者信息

Ohkubo I, Namikawa C, Higashiyama S, Sasaki M, Minowa O, Mizuno Y, Shiokawa H

机构信息

Department of Biochemistry, Nagoya City University Medical School, Japan.

出版信息

Int J Biochem. 1988;20(3):243-58. doi: 10.1016/0020-711x(88)90348-5.

Abstract
  1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.
摘要

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