Comparative studies on proteasomes (multicatalytic proteinases) isolated from spermatozoa and eggs of sea urchins.
1. Proteasomes (multicatalytic proteinases) have been purified from spermatozoa and eggs of sea urchins by successive chromatographies on DEAE-cellulose, hydroxylapatite, and Sepharose 6B. 2. The isolated sperm and egg proteasomes showed similar properties such as molecular weight (both 630,000) and multiple catalytic activity (pH optimum, substrate specificity, inhibitor-susceptibility and SDS-stimulation). 3. Distinct protein components were detected between sperm and egg proteasomes by SDS-polyacrylamide gel electrophoresis and immunoblot analysis using antibody against egg proteasome.
Saitoh
Y
Y
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Kawahara
H
H
Miyamatsu
H
H
Yokosawa
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D015151:Immunoblotting; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000302:isolation & purification; D010063:Ovum / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex; D012617:Sea Urchins / Q000737:chemistry; D013094:Spermatozoa / Q000201:enzymology*; D013379:Substrate Specificity
D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex