Proteins from the sperm of the bivalve mollusc Ensis minor
- 1 November 1983
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 136 (3) , 509-516
- https://doi.org/10.1111/j.1432-1033.1983.tb07770.x
Abstract
Analysis of the total protein of the mature sperm of the bivalve mollusc Ensis minor (razor shell) using gel electrophoresis, amino acid analysis, nuclear magnetic resonance, circular dichroism and trypsin digestion, show it to contain all five histones plus a protamine‐like protein. The histones H3, H4 and probably H2A are similar to those from calf thymus or sea urchin sperm, but the putative H2B appears to have a very high molecular mass (about 20kDa). The histone H1 molecule is unusual, having little or no proline and 8–10 residues of histidine. The protamine‐like species is rich in both lysine as well as arginine and is of much higher molecular mass than fish sperm protamines. Nucleosomes containing the four core histones have been prepared and the nucleosomal repeat shown to be 200 ± 5 base pairs. Checks for the absence of contaminating cells reinforce the conclusion that a histone‐containing nucleθsomal structure co‐exists with a protamine‐like protein in this sperm chromatin.This publication has 28 references indexed in Scilit:
- Nuclear proteins and the organization of chromatin in spermatozoa of Mythus edulisExperimental Cell Research, 1982
- Presence of H2b histone in spermatozoa from marine gastropodaExperimental Cell Research, 1981
- Electron microscope evidence for the presence of globular structures in different sperm chromatins.The Journal of cell biology, 1980
- Electrophoretic analysis of nuclear proteins isolated from sperm of the black abalone Haliotis crackeroidiiExperimental Cell Research, 1979
- More histone structuresFEBS Letters, 1979
- Action of micrococcal nuclease on chromatin and the location of histone H1Journal of Molecular Biology, 1977
- Conformational changes in subfractions of calf thymus histone H1Biochemistry, 1976
- Studies on the Role and Mode of Operation of the Very-Lysine-Rich Histones in Eukaryote Chromatin. The Conformation of phi 1 Histones from Marine Invertebrate SpermEuropean Journal of Biochemistry, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970