PURIFICATION AND CHARACTERIZATION OF PROGESTERONE-BINDING GLOBULIN IN THE PREGNANT CAPE PORCUPINE, HYSTRIX AFRICAEAUSTRALIS

被引：1

作者：

VANWYK, V

NEITZ, AWH

LOUW, AI

VANAARDE, RJ

机构：

[1] UNIV PRETORIA,DEPT BIOCHEM,PRETORIA 0002,SOUTH AFRICA

[2] UNIV PRETORIA,DEPT ZOOL,MAMMAL RES INST,PRETORIA 0002,SOUTH AFRICA

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-PHARMACOLOGY TOXICOLOGY & ENDOCRINOLOGY | 1995年 / 111卷 / 02期

关键词：

PROGESTERONE-BINDING; GLOBULIN; CAPE PORCUPINE; HYSTRIX AFRICAEAUSTRALIS; PURIFICATION; CHARACTERIZATION;

D O I：

10.1016/0742-8413(95)00013-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Progesterone-binding globulin (PEG) was purified from pooled pregnant Cape porcupine (Hystrix africaeaustvalis) plasma by SP-Sephadex chromatography, followed by Sephacryl S-200 gel filtration, The final product was homogeneous according to high performance capillary electrophoresis, SDS-polyacrylamide gel electrophoresis and sedimentation equilibrium centrifugation, A molecular mass of 65,300 Da was calculated from sedimentation equilibrium centrifugation data. Scatchard analysis indicated a dissociation constant of 0.82 x 10(-9) M, and PEG concentration of 18.4 nmole/mg protein.

引用

页码：175 / 181

页数：7

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