PMID: 3743878Jan 1, 1986Paper

Alanyl aminopeptidase of bovine seminal vesicle secretion

The International Journal of Biochemistry
Y Agrawal, T Vanha-Perttula

Abstract

Multiple forms of an aminopeptidase hydrolysing L-alanine- and various other amino acid-beta-naphthylamides in bovine seminal vesicle secretion were studied after fractionation on gel filtration, anion exchange chromatography and chromatofocusing. Two forms of the enzyme were found in all these fractionations: one with a high molecular weight was aggregated or particle-bound and the other had a molecular weight of about 237,000. The high-molecular-weight form dissociated with Triton X-100 via an intermediate into the basic enzyme form with concurrent change in the pI and anionic sites. The basic form of the enzyme differed from the high-molecular-weight forms in substrate preference, response to some modifiers, thermal stability and kinetic constants.

References

Jan 1, 1986·The International Journal of Biochemistry·Y Agrawal, T Vanha-Perttula
Jun 1, 1985·International Journal of Andrology·Y Agrawal, T Vanha-Perttula
Jan 1, 1985·The International Journal of Biochemistry·K LaluT Vanha-Perttula
Jul 30, 1974·Biochemistry·C W Garner, F J Behal
Nov 1, 1974·The Journal of Cell Biology·D S Friend, D W Fawcett
Oct 1, 1969·Journal of Reproduction and Fertility·J SuominenM Niemi
Feb 1, 1972·Journal of Reproduction and Fertility·S Meizel, J Cotham
Jan 1, 1967·Archiv für klinische und experimentelle Dermatologie·V K Hopsu-Havu, K K Mäkinen
Jan 1, 1983·The International Journal of Biochemistry·T Vanha-Perttula, A Jauhiainen

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Citations

Oct 14, 1988·Clinica Chimica Acta; International Journal of Clinical Chemistry·T Vanha-Perttula
Jun 9, 2004·Reproduction in Domestic Animals = Zuchthygiene·R El-Hajj GhaouiW M C Maxwell
Aug 1, 1989·International Journal of Andrology·Y P Agrawal, T Vanha-Perttula
Dec 1, 1986·International Journal of Andrology·Y Agrawal, T Vanha-Perttula
May 1, 2021·Animals : an Open Access Journal From MDPI·María Pilar Viudes-de-CastroClara Marin

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