Studies on protease of the rotifer Brachionus plicatilis - I. Purification of alkaline protease of the rotifer Brachionus plicatilis.

1 January 1984

journal article
Published by Japanese Society of Fisheries Science in NIPPON SUISAN GAKKAISHI

Vol. 50 (9) , 1605-1609
https://doi.org/10.2331/suisan.50.1605

Abstract

Alkaline proteases were isolated from the crude extract of the rotifer Brachionus plicatilis by the combination of gel filtration and ion-exchange chromatogaphy. Two-main active fractions, designated as F-I and F-II, were eluted on the second DEAE-cellulose column, and F-I was finally purified about 190-fold and F-II about 920-fold. F-II was homogeneous as judged from polyacrylamide disc gel electrophoresis. The molecular weihts of F-I and F-II were estimated to be about 800, 000 and 900, 000, respectively, by Sepharose 6B gel filtration, and their isoelectric points were found to be 9.7 and 5.6, respectively.

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