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Purification and partial amino acid sequence of initiatorin, a prostatic endopeptidase of the silkworm, Bombyx mori
Authors:Toshiro Aigaki  Hiroko Kasuga  Sumiharu Nagaoka and Minoru Osanai
Institution:

a Department of Experimental Biology, Tokyo Metropolitan Institute of Gerontology. Sakaecho 35-2, Itabashi-ku, Tokyo 173, Japan

b Department of Sericultural Science, Faculty of Agriculture, Kyushu University, Hakozaki 6-10-1, Fukuoka, Japan

c Department of Biology, Faculty of Science, Kanazawa University, Kakamamachi, Kanazawa, Japan

Abstract:We have purified initiatorin, a prostatic endopeptidase that initiates the protein-arginine degradation cascade in the spermatophore of Bombyx mori. Purification of the enzyme from spermatophores was monitored by measuring BAEE (Ngreek small letter alpha-benzoyl-Image -arginine-ethyl ester) hydrolyzing activity. Spermatophores were used as a source for this enzyme. Of several isoforms the major form (MW, 29 kDa) was purified over 200-fold. The N-terminal sequence of initiatorin showed strong homology with those of serine-type of endopeptidases.
Keywords:Endopeptidase  Initiatorin  Prostatic gland  Spermatophore  Apyrene spermatozoa activating factor (AAF)  Bombyx mori
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