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Anionic and cationic components from protein aggregates in bovine seminal plasma and their effects of sperm motility
Author(s) -
AlSomai N.,
C. Molan P.,
Vishwanath R.,
Shan P.
Publication year - 1994
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1080390310
Subject(s) - cationic polymerization , motility , molecular mass , gel permeation chromatography , sperm , biology , peptide , sperm motility , chromatography , biophysics , size exclusion chromatography , biochemistry , chemistry , microbiology and biotechnology , polymer chemistry , organic chemistry , enzyme , botany , polymer
Bovine seminal plasma proteins are in an aggregated form of high molecular weight in their native state. By immobilisation on a cation exchanger with exposure to disaggregating conditions (i.e., acetonitrile and low pH), the high‐molecular‐weight aggregates could be dissociated to slowly release the low‐molecular‐weight components. The anionic component released from the cation exchanger during disaggregation was collected by adsorption on a hydrophobic interaction column. The cationic component remaining on the cation exchanger was eluted with NaOH. Both components were found on gel permeation chromatography to be <5 kDa. SDS—PAGE of the various fractions showed that component of low molecular weight were still in an aggregated form. These components resulting from the disaggregation process have detrimental effects on sperm motility and the effects were more substantial compared with that of whole seminal plasma. All the cationic components were significantly detrimental to sperm motility, especially the fractions of low molecular weight. The anionic fractions reduced sperm motility when in an aggregated state. The isolated anionic peptide was not detrimental in its free form. In all fractions the peptides tended to re‐aggregate to a higher molecular weight under neutral conditions, however, the isolated anionic peptide (molecular weight <1,500) failed to do so. © Wiley‐Liss, Inc.