TY - JOUR
T1 - Bovine sperm forward motility protein. Partial purification and characterization
AU - Acott, T. S.
AU - Hoskins, D. D.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1978
Y1 - 1978
N2 - A protein, present in bovine seminal plasma, initiates forward motility in immature, immotile caput spermatozoa that have been incubated with a cyclic AMP phosphodiesterase inhibitor. An improved motility assay was developed to study this process and the protein involved. This forward motility protein exhibits multiple forms when fractionated on the basis of charge or molecular weight. Molecular sieving in urea or sodium dodecyl sulfate and dithiothreitol results in a single peak of activity which will re-form the larger aggregates in the absence of these agents. The molecular weight of this monomeric motility protein, as estimated from molecular sieving under these dissociating conditions, is 37,500. The forward motility protein can be partially purified by heat treatment, gel chromatography in urea, and affinity chromatography on concanavalin A/agarose. Enzymatic treatments further suggest a glycoprotein nature, i.e. treatment with β-galactosidase, neuraminidase, α-mannosidase, or galactose oxidase reduces its activity by 50%; treatment with trypsin completely abolishes forward motility protein activity. On the basis of concurrent studies on the activity, properties, and distribution of forward motility protein in bovine body fluids, it is suggested that this protein is involved in the development of the capacity for motility as sperm traverse the epididymis.
AB - A protein, present in bovine seminal plasma, initiates forward motility in immature, immotile caput spermatozoa that have been incubated with a cyclic AMP phosphodiesterase inhibitor. An improved motility assay was developed to study this process and the protein involved. This forward motility protein exhibits multiple forms when fractionated on the basis of charge or molecular weight. Molecular sieving in urea or sodium dodecyl sulfate and dithiothreitol results in a single peak of activity which will re-form the larger aggregates in the absence of these agents. The molecular weight of this monomeric motility protein, as estimated from molecular sieving under these dissociating conditions, is 37,500. The forward motility protein can be partially purified by heat treatment, gel chromatography in urea, and affinity chromatography on concanavalin A/agarose. Enzymatic treatments further suggest a glycoprotein nature, i.e. treatment with β-galactosidase, neuraminidase, α-mannosidase, or galactose oxidase reduces its activity by 50%; treatment with trypsin completely abolishes forward motility protein activity. On the basis of concurrent studies on the activity, properties, and distribution of forward motility protein in bovine body fluids, it is suggested that this protein is involved in the development of the capacity for motility as sperm traverse the epididymis.
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M3 - Article
C2 - 211130
AN - SCOPUS:0018117203
SN - 0021-9258
VL - 253
SP - 6744
EP - 6750
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 19
ER -