Studies on acrosin. I. Purification and characterization of boar acrosin.
@article{Kaneko1981StudiesOA, title={Studies on acrosin. I. Purification and characterization of boar acrosin.}, author={Sachiko Kaneko and Chiaki Moriwaki}, journal={Journal of pharmacobio-dynamics}, year={1981}, volume={4 1}, pages={ 20-7 } }
Acrosin was extracted from boar sperm and purified by Sephadex gel filtration and affinity chromatography on Phe-Phe-Arg Sepharose 4B in acidic condition. Its enzymic properties were characterized in comparison with trypsin. The oligopeptides with Arg at the carboxy-termini were used as the ligands for affinity chromatography. Phe-Phe-Arg adsorbed acrosin at pH 5 and released in at pH 3. To adsorb acrosin, it was found that the ligand should be longer than tripeptide with Arg in the carboxy…
11 Citations
Human acrosin: purification and some properties.
- Biology, ChemistryArchives of andrology
- 1991
Human sperm with normal morphology and good viability were obtained by centrifugation using a discontinuous Percoll density gradient with an inner column and human acrosin showed a broad substrate specificity for arginine and lysine derivatives and it seemed to have a somewhat different specificity from trypsin.
Enzymatic action of basic arginine amidases in human seminal plasma.
- BiologyArchives of andrology
- 1992
Three basic arginine amidases with different affinities to lima bean trypsin inhibitor (LBTI) and aprotinin affinity columns were separated in the middle molecular weight (MMW) preparation obtained…
Basic arginine esterase from human seminal plasma: purification and some properties.
- Biology, ChemistryArchives of andrology
- 1991
The enzymatic characteristics of present enzyme were clearly different from tissue kallikrein, acrosin, and seminin in human semen.
Studies on dipeptidyl carboxypeptidase in the male reproductive organs; its biological and pathological status.
- Biology, ChemistryJournal of pharmacobio-dynamics
- 1981
It is supposed that dipeptidyl carboxypeptidase in male genital organ and its secretion seem to be related to the male reproductive functions.
Human seminal plasma proteinase inhibitor: action toward some trypsin-like arginine amidases from humans.
- Biology, ChemistryArchives of andrology
- 1993
Measurement of Ki values of BHSAA-L with affinity to LBTI column toward HSTPI revealed that the arginine amidase had a stronger affinity for LBTi than that for H STPI, indicating that it is the difference in Ki values that allows BHS AA-L to be separated by the L BTI affinity adsorption method from human seminal plasma containing a large amount of HST PI.
Effects of kinins and dipeptidyl carboxypeptidase on the motility of highly washed human sperm.
- Biology, ChemistryJournal of pharmacobio-dynamics
- 1981
Dipeptidyl carboxypeptidase level in ejaculated human semen was found to correlate to the semen quality, such as sperm density and motility, but it gave no direct influence on sperm motility.
Trypsin-like arginine amidases including plasminogen and plasmin in human seminal plasma by affinity adsorption and elution.
- Biology, ChemistryArchives of andrology
- 1992
Two kinds of trypsin-like basic arginine amidase activity were also separated by the above-mentioned affinity adsorptions from a CM-cellulose-adsorbed preparation of human seminal plasma.
Two forms of basic trypsin-like arginine amidases in boar sperm.
- BiologyArchives of andrology
- 1993
Acrosin and newly detected basic arginine amidase were separated from boar sperm by affinity adsorption using lima bean trypsin inhibitor (LBTI) and aprotinin columns, respectively. These enzymes…
Detection and separation of two kinds of acidic arginine amidases from boar sperm using lima bean trypsin inhibitor and aprotinin affinity adsorptions.
- Biology, ChemistryArchives of andrology
- 1992
Two kinds of acidic arginine amidase activity were found in boar sperm and were separated by a treatment consisting of lima bean trypsin inhibitor affinity adsorption and elution, and profiles of their substrate specificities were different.
Immunocytochemical and enzyme histochemical localization of kallikrein-like enzymes in colon, intestine, and stomach of rat and cat.
- BiologyThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
- 1986
Modification in the enzyme histochemical procedure (pH, fixation) yielded positive results for a kallikrein-like protease in goblet cells of the intestine and colon, which may have physiological and pathological significance in the gastrointestinal tract.
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