THE PROBLEM OF PLASTEIN FORMATION: I. THE FORMATION OF A PLASTEIN BY PAPAIN

Author:

Collier H. B.

Abstract

Papain, activated by cyanide, cysteine, or hydrogen sulphide, produces a plastein, a protein-like substance, from concentrated peptic or papain digests of egg albumin. This activity is suppressed by boiling, aeration, the addition of copper salts, hydrogen peroxide, iodoacetate, or alloxan, indicating that free SH groups are essential. The optimum pH for plastein formation is 4.8; that for hydrolysis of the plastein by papain is about pH 4.2. It is concluded that concentration alone controls the direction of the enzyme action, the optimum pH and oxidation-reduction conditions being practically identical for both formation and hydrolysis of plastein.The rate of plastein formation varies with substrate concentration, above a minimum value. With constant substrate concentration, the rate of plastein formation varies as the square-root of the enzyme concentration. Hydroxylamine reduces the activity of the papain by about one-half. A similar effect is produced by treatment with phenylhydrazine, followed by benzaldehyde. Phenylhydrazine alone has no effect, whereas benzaldehyde alone depresses the activity very strongly.

Publisher

Canadian Science Publishing

Subject

Pharmacology (medical),Complementary and alternative medicine,Pharmaceutical Science

Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Nitrogen Metabolism of Higher Plants;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

2. Proteinase-Catalyzed Synthesis of Peptide Bonds;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

3. Modification of leaf protein concentrate by the use of plastein reaction;Journal of the Science of Food and Agriculture;1979-09

4. CHARACTERIZATION OF PLASTEIN REACTION PRODUCTS FORMED BY PEPSIN, ?-CHYMOTRYPSIN, AND PAPAIN TREATMENT OF EGG ALBUMIN HYDROLYSATES;Journal of Food Science;1978-07

5. A light scattering investigation of the interaction of pepsin with bovine serum albumin;Archives of Biochemistry and Biophysics;1962-02

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