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DIFFERENCES IN ASSOCIATION OF CORTICOSTEROIDS WITH SERUM PROTEINS OF DIFFERENT ANIMAL TYPES
Author(s) -
Reich Magda
Publication year - 1960
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1960.19
Subject(s) - corticosterone , corticosteroid , albumin , transcortin , endocrinology , medicine , hormone , blood proteins , steroid , globulin , bovine serum albumin , serum albumin , animal species , biology , gel electrophoresis , chemistry , biochemistry , zoology
SUMMARY A marked species difference in the capacity of plasma protein fractions to combine with corticosteroids has been demonstrated by the use of C 14 ‐labelled cortisol and corticosterone, and paper electrophoresis methods. Of the five species studied, human serum had the highest and sheep serum the lowest capacity for corticosteroid binding. Studies made on the properties of corticosteroid protein complexes showed that the eluted corticosteroids were unaltered physically; there was an interchange between the bound and added corticosteroid; there was no competition for sites between the individual corticosteroids. It was shown in human sera that, at maximum binding between corticosterone‐4‐C 14 and albumin, approximately 5 albumin molecules per 1 corticosterone molecule were involved. The findings indicate the complexity of the characteristics of the protein carrier mechanism for steroid hormones in diverse animal species.