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Partial characterization of a proacrosin binding protein *
Author(s) -
Yi L. S. H.,
Runion C. M.,
Willand J. L.,
Polakoski K. L.
Publication year - 2009
Publication title -
andrologia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.633
H-Index - 59
eISSN - 1439-0272
pISSN - 0303-4569
DOI - 10.1111/j.1439-0272.1992.tb02607.x
Subject(s) - chemistry , biochemistry , protein a/g , gel electrophoresis , binding protein , polyacrylamide gel electrophoresis , electrophoresis , gelatin , protein g , acrosin , amino acid , chromatography , acrosome , biology , sperm , enzyme , recombinant dna , antibody , botany , immunology , fusion protein , gene
Summary. All of the acid (pH 4.0) extracted proacrosin from porcine epididymal spermatozoa was found to be tightly associated with a specific protein referred to as the binding protein. A combination of gel filterations and gel electrophoresis revealed that the binding protein is composed of a major 28 kd and a minor 29 kd protein. Both of the proteins were shown to be non‐proteolytic by gelatin SDS‐PAGE analysis and the amino acid composition analysis of the purified 28 kd protein revealed that it is not related to the proteolytic component of the proacrosin‐acrosin system.