Subunits of human plasma kininase II generated by plasma kallikrein
| Autor: | Nakahara Masao |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Plasmin
Trypsin inhibitor Protein subunit Bradykinin In Vitro Techniques Peptidyl-Dipeptidase A Biochemistry chemistry.chemical_compound medicine Humans Lysine Carboxypeptidase Pharmacology Chemistry Proteolytic enzymes Kallikrein Trypsin Molecular biology Angiotensin II Peptide Fragments Molecular Weight Chromatography Gel Kallikreins Peptide Hydrolases medicine.drug |
| Zdroj: | Biochemical Pharmacology. 27:1651-1657 |
| ISSN: | 0006-2952 |
| DOI: | 10.1016/0006-2952(78)90174-0 |
| Popis: | Partially purified human plasma kininase II was incubated with proteolytic enzymes such as plasma kallikrein, prekallikrein activator, plasmin, thrombin and trypsin. Digestion of plasma kininase II by plasma kallikrein generated 180,000 (I) and 95,000 (II) mol. wt subunits while plasmin, thrombin and trypsin inactivated plasma kininase II. These subunits have two activities just as plasma kininase has: they hydrolyze bradykinin, and they convert angiotensin I into angiotensin II. K m values of the two subunits for bradykinin were 0.17 × 10 −6 M, indicating that this value was identical with plasma kininase II. V max values of the two subunits for bradykinin were higher than that of plasma kininase II. The bradykininase activities of the two subunits were significantly inhibited by inhibitors such as HgCl 2 , ethylenediamine tetraacetic acid. p -chloromercuriphenyl sulfonic acid, SQ 20881(BPF9a), soy bean trypsin inhibitor and Trasylol. The behaviour of the two subunits towards these above inhibitors was also identical with plasma kininase II. A 180,000 mol. wt kininase was partially purified from human plasma. The kininase had bradykinin-inactivating and angiotensin I-converting activities. Its K m value and the behaviour towards the inhibitors described above were the same as the subunit I. |
| Databáze: | OpenAIRE |
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