Boar proacrosin is a single‐chain molecule which has the N‐terminus of the acrosin A‐chain (light chain)
- 5 December 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 241 (1-2) , 136-140
- https://doi.org/10.1016/0014-5793(88)81046-9
Abstract
Boar proacrosin was isolated from spermatozoa by a novel procedure under conditions preventing proenzyme activation. The spermatozoal extract was fractionated by gel filtration and reversed-phase FPLC, all in acidic solutions. Isolated proacrosin had a molecular mass of 55/53 kDa (doublet) and was devoid of amidolytic activity. Its single N-terminal sequence corresponded to that of the 23-residue acrosin A-chain and continued with that of the acrosin B-chain. Autoactivation at pH 7.8 did not influence the molecular mass. However, activated material contained two parallel N-terminal sequences, those of the A- and B-chain. Thus, activation of proacrosin is analogous to that of other serine proteinase proenzymes.Keywords
This publication has 15 references indexed in Scilit:
- Carbohydrate-binding properties of boar sperm proacrosin and assessment of its role in sperm-egg recognition and adhesion during fertilizationDevelopment, 1988
- Zona Pellucida-Binding and Fucose-Binding of Boar Sperm Acrosin is Not Correlated with Proteolytic ActivityBiological Chemistry Hoppe-Seyler, 1988
- Acrosin shows zona and fucose binding, novel properties for a serine proteinaseFEBS Letters, 1987
- Biochemical and immunological comparisons between the human and boar proacrosin-acrosin proteinase systemsJournal of Reproductive Immunology, 1987
- Computer-assisted determination of protein concentrations from dye-binding and bicinchoninic acid protein assays performed in microtiter platesJournal of Immunological Methods, 1986
- Biochemical studies on proacrosin and acrosin from epididymal boar spermatozoa: In vitro translation of boar testicular proacrosin mRNABiochemical and Biophysical Research Communications, 1986
- Boar acrosin is a two-chain molecule. Isolation and primary structure of the light chain; homology with the pro-part of other serine proteinasesEuropean Journal of Biochemistry, 1984
- Boar Acrosin. Isolation of Two Active Forms from Boar Ejaculated SpermHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1982
- N-Terminal Amino Acid Sequence of Boar Sperm Acrosin. Homology with Other Serine ProteinasesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- Purification and Properties of Boar AcrosinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980