Literature DB >> 7204534

Relaxin purification from human placental basal plates.

S Yamamoto, S C Kwok, F C Greenwood, G D Bryant-Greenwood.   

Abstract

A crude relaxin preparation has been obtained from the basal plate region of electric cesarean section human placentae, as well as normal term placentae. The relaxin isolated has different charge properties by ion exchange chromatography from porcine relaxin, although it is of approximately the same molecular size. The most potent fraction obtained has approximately 0.7% of the immunoactivity of purified porcine relaxin when compared with porcine relaxin in a RIA based on porcine material, suggesting significant amino acid sequence differences between the putative human relaxin and its porcine counterpart.

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Year:  1981        PMID: 7204534     DOI: 10.1210/jcem-52-4-601

Source DB:  PubMed          Journal:  J Clin Endocrinol Metab        ISSN: 0021-972X            Impact factor:   5.958


  2 in total

1.  Expression and Characterization of Relaxin Family Peptide Receptor 1 Variants.

Authors:  David Speck; Gunnar Kleinau; Mark Meininghaus; Antje Erbe; Alexandra Einfeldt; Michal Szczepek; Patrick Scheerer; Vera Pütter
Journal:  Front Pharmacol       Date:  2022-01-28       Impact factor: 5.810

2.  Relaxin gene expression in human ovaries and the predicted structure of a human preprorelaxin by analysis of cDNA clones.

Authors:  P Hudson; M John; R Crawford; J Haralambidis; D Scanlon; J Gorman; G Tregear; J Shine; H Niall
Journal:  EMBO J       Date:  1984-10       Impact factor: 11.598

  2 in total

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