Studies on acrosin. I. Purification and characterization of boar acrosin.

  title={Studies on acrosin. I. Purification and characterization of boar acrosin.},
  author={Sachiko Kaneko and Chiaki Moriwaki},
  journal={Journal of pharmacobio-dynamics},
  volume={4 1},
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.


Multiple forms of human acrosin: isolation and properties.
The relationship between the occurrence of multiple acrosin forms and proenzyme activation by limited proteolysis is discussed.
Effects of acrosin inhibitors on the soluble and membrane-bound forms of ram acrosin, and a reappraisal of the role of the enzyme in fertilization.
  • C. BrownE. Hartree
  • Biology, Chemistry
    Hoppe-Seyler's Zeitschrift fur physiologische Chemie
  • 1976
It is proposed that membrane-bound acrosin is the form that functions in penetration of the zona pellucida, and that a role for acrosIn inhibitors is suppression of an antifertility effect of soluble acros in mammalian eggs.
Properties of acrosomal hyaluronidase from bull spermatozoa. Evidence for its similarity to testicular hyaluronidase.
The results suggest that sperm acrosomal hyaluronidase is identical with testicular hyalurinidase but is apparently different from lysosomal hyAluronid enzyme, present in organs other than the testis.
Occurrence of multiple forms of bull and ram acrosin during proenzyme activation and inhibition of activation by p-nitrophenyl p'-guanidinobenzoate.
Proacrosin activation was completely prevented in the presence of 10(-4) M p-nitrophenyl p'-guanidinobenzoate, and the protein pattern of such activation samples was determined after sodium dodecylsulfate-polyacrylamide gel electrophoresis.
Amino Acid Content of Rabbit Acrosomal Proteinase and Its Similarity to Human Trypsin
Rabbit acrosomal proteinase from epididymal spermatozoa of 44 male rabbits was purified by subcellular fractionation, sucrose density gradient centrifugation, and electrofocusing; the specific activity of the purified product was similar to that observed for pancreatic trypsins from various sources.
Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads.
  • P. Cuatrecasas
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1970
It is demonstrated that successful application of affinity chromatography in many cases will critically depend on placing the ligand at a considerable distance from the matrix backbone.
Relationship of a trypsin-like enzyme in rabbit spermatozoa to capacitation.
The existence of a trypsin-like enzyme (TLE) in acrosomes ofepididymal spermatozoa was confirmed and was further demonstrated to be present in acrosomes of ejaculated and capacitated spermatozoa. TLE
Acrosomal Proteinase and Proteinase Inhibitor of Human Spermatozoa
The acrosomal proteinase of human spermatozoa was characterized and differs from other human proteinases, which has optimal activity at pH 8.0, and possesses a proteinase inhibitor that is similar to one of the proteinase inhibitors from human seminal plasma.
Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors.
Capacitated rabbit spermatozoa were treated with pancreatic trypsin inhibitor or partially purified seminal plasma trypsin inhibitor. Subsequent insemination of the spermatozoa into the oviducts of