Antimutagenic Activity of 5.ALPHA.-Cholest-7-en-3.BETA.-ol, a New Component from the Starfish Asterina pectinifera.

The sterols of the echinoderm Asterias rubens.

1. Twenty-two sterols were identified in the starfish Asterias rubens (Phylum, Echinodermata; Class, Asteroidea). 2. The major 4-demethyl sterols had a Delta(7) bond and the C(27) compound 5alpha-cholest-7-en-3beta-ol predominated over other mono- and di-unsaturated sterols belonging to the C(26), C(27), C(28) and C(29) series. 3. Small amounts of cholest-5-en-3beta-ol and 5alpha-cholestan-3bet...

Isolation and characteristics of trypsin from pyloric ceca of the starfish Asterina pectinifera.

Trypsin was purified from pyloric ceca of the starfish Asterina Pectinifera by ammonium sulfate precipitation, gel filtration, and cation-exchange chromatography. Final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 28000. Optimum pH and temperature of A. pectinifera trypsin for hydro...

Isolation and characteristics of phospholipase A2 from the pyloric ceca of the starfish Asterina pectinifera

Studies on dwarf larvae developed from isolated blastomeres of the starfish. Asterina pectinifera.

Not only a whole denuded egg, but also blastomeres isolated from 2-, 4- and 8-cell starfish embryos developed into morphologically normal, but dwarf bipinnariae, the sizes of which were roughly proportionate to that of the respective original blastomeres. Some of the blastomeres isolated from the 16-cell stage were also capable of developing into the larval stage. All isolated blastomeres divid...

Characterization of a novel hatching enzyme purified from starfish Asterina pectinifera

Hatching enzyme is a protease which can degrade the membrane of egg. In this study, a hatching enzyme was purified from starfish (Asterina pectinifera) with 6.34 fold of purification rate, 5.04 % of yield, and 73.87 U/mg of specific activity. The molecular weight of starfish hatching enzyme was 86 kDa, which was reduced to 62 kDa after removal of N-linked oligosaccharides. The optimal pH and te...