Literature DB >> 4422648

Amino acid content of rabbit acrosomal proteinase and its similarity to human trypsin.

R Stambaugh, M Smith.   

Abstract

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 20,047 units per milligram, a value similar to that observed for pancreatic trypsins from various sources. The molecular weight determined from the amino acid analyses and ultracentrifugation was about 22,000. This rabbit acrosomal proteinase showed great similarity to pancreatic trypsin, especially to human pancreatic trypsin, both in the number of individual amino acids and in the total number of residues. This similarity was confirmed by an antigenic cross reaction between rabbit antiserum to bovine pancreatic trypsin with human, rabbit, rhesus monkey, and bull acrosotnal proteinase.

Entities:  

Mesh:

Substances:

Year:  1974        PMID: 4422648     DOI: 10.1126/science.186.4165.745

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  3 in total

1.  Heparin-sepharose affinity chromatography for purification of bull seminal-plasma hyaluronidase.

Authors:  P N Srivastava; A A Farooqui
Journal:  Biochem J       Date:  1979-12-01       Impact factor: 3.857

2.  Studies on ram acrosin. Activation of proacrosin accompanying the isolation of acrosin from spermatozoa, and purification of the enzyme by affinity chromatography.

Authors:  C R Brown; E F Hartree
Journal:  Biochem J       Date:  1978-10-01       Impact factor: 3.857

3.  Characterization of a high-molecular-weight form of human acrosin. Comparison with human pancreatic trypsin.

Authors:  R A Anderson; S A Beyler; S R Mack; L J Zaneveld
Journal:  Biochem J       Date:  1981-11-01       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.