Proteins from the sperm of the bivalve mollusc Ensis minor. Co-existence of histones and a protamine-like protein
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...
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| Veröffentlicht in: | European journal of biochemistry 1983-11, Vol.136 (3), p.509-516 |
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| container_title | European journal of biochemistry |
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| creator | Giancotti, V Russo, E Gasparini, M Serrano, D Del Piero, D Thorne, A W Cary, P D Crane-Robinson, C |
| description | 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 20 kDa). 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 nucleosomal structure co-exists with a protamine-like protein in this sperm chromatin. |
| doi_str_mv | 10.1111/j.1432-1033.1983.tb07770.x |
| format | Article |
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Co-existence of histones and a protamine-like protein</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Giancotti, V ; Russo, E ; Gasparini, M ; Serrano, D ; Del Piero, D ; Thorne, A W ; Cary, P D ; Crane-Robinson, C</creator><creatorcontrib>Giancotti, V ; Russo, E ; Gasparini, M ; Serrano, D ; Del Piero, D ; Thorne, A W ; Cary, P D ; Crane-Robinson, C</creatorcontrib><description>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 20 kDa). 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. 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Co-existence of histones and a protamine-like protein</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>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 20 kDa). 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 nucleosomal structure co-exists with a protamine-like protein in this sperm chromatin.</description><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>biochemical analysis</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>chromatin</subject><subject>Circular Dichroism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Ensis minor</subject><subject>histones</subject><subject>Histones - isolation & purification</subject><subject>Hydrogen-Ion Concentration</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Male</subject><subject>Marine</subject><subject>Mollusca - metabolism</subject><subject>protamine</subject><subject>Protamines - isolation & purification</subject><subject>proteins</subject><subject>Proteins - isolation & purification</subject><subject>spermatozoa</subject><subject>Spermatozoa - analysis</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUUtPwzAMjhBojMFPQIo4cGuJm5I03NA0HtIkOMA5alNXy2ibrWmn8e9pt2pXfLEtfw_JHyF3wELo62EdQsyjABjnIaiEh23GpJQs3J-R6el0TqaMQRxE6lFckivv14wxoYSckIkQMcgomZLtZ-NatLWnReMq2q6Q-g02FXXFYcnsLi13SCtXlp03dFF762lla9eEdO4C3FvfYm1wIKz62dXoaVrnNKWbXjrtoRiU9gcPa-90TS6KtPR4M_YZ-X5ZfM3fguXH6_v8eRmYiPE2EKAwjpFnKAxHCQbiSAhIJVMCsjxmgLlKmBHMABYi55DxPDcJx0jlSWT4jNwfdXvfbYe-1ZX1BssyrdF1XidMcim4-BcIXEZKyQH4dASaxnnfYKE3ja3S5lcD00Mweq2H7-vh-3oIRo_B6H1Pvh1duqzC_EQdk-B_5ZiMBA</recordid><startdate>19831115</startdate><enddate>19831115</enddate><creator>Giancotti, V</creator><creator>Russo, E</creator><creator>Gasparini, M</creator><creator>Serrano, D</creator><creator>Del Piero, D</creator><creator>Thorne, A W</creator><creator>Cary, P D</creator><creator>Crane-Robinson, C</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19831115</creationdate><title>Proteins from the sperm of the bivalve mollusc Ensis minor. Co-existence of histones and a protamine-like protein</title><author>Giancotti, V ; Russo, E ; Gasparini, M ; Serrano, D ; Del Piero, D ; Thorne, A W ; Cary, P D ; Crane-Robinson, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c203t-619e44e3be6c3e71c142661a70961bd401ed980c60c1ef6d31b3ddc83e29d82c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>biochemical analysis</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>chromatin</topic><topic>Circular Dichroism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Ensis minor</topic><topic>histones</topic><topic>Histones - isolation & purification</topic><topic>Hydrogen-Ion Concentration</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Male</topic><topic>Marine</topic><topic>Mollusca - metabolism</topic><topic>protamine</topic><topic>Protamines - isolation & purification</topic><topic>proteins</topic><topic>Proteins - isolation & purification</topic><topic>spermatozoa</topic><topic>Spermatozoa - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Giancotti, V</creatorcontrib><creatorcontrib>Russo, E</creatorcontrib><creatorcontrib>Gasparini, M</creatorcontrib><creatorcontrib>Serrano, D</creatorcontrib><creatorcontrib>Del Piero, D</creatorcontrib><creatorcontrib>Thorne, A W</creatorcontrib><creatorcontrib>Cary, P D</creatorcontrib><creatorcontrib>Crane-Robinson, C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Giancotti, V</au><au>Russo, E</au><au>Gasparini, M</au><au>Serrano, D</au><au>Del Piero, D</au><au>Thorne, A W</au><au>Cary, P D</au><au>Crane-Robinson, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteins from the sperm of the bivalve mollusc Ensis minor. Co-existence of histones and a protamine-like protein</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1983-11-15</date><risdate>1983</risdate><volume>136</volume><issue>3</issue><spage>509</spage><epage>516</epage><pages>509-516</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><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 20 kDa). 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 nucleosomal structure co-exists with a protamine-like protein in this sperm chromatin.</abstract><cop>England</cop><pmid>6641728</pmid><doi>10.1111/j.1432-1033.1983.tb07770.x</doi><tpages>8</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 1983-11, Vol.136 (3), p.509-516 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Animals biochemical analysis Chemical Phenomena Chemistry chromatin Circular Dichroism Electrophoresis, Polyacrylamide Gel Ensis minor histones Histones - isolation & purification Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Male Marine Mollusca - metabolism protamine Protamines - isolation & purification proteins Proteins - isolation & purification spermatozoa Spermatozoa - analysis |
| title | Proteins from the sperm of the bivalve mollusc Ensis minor. Co-existence of histones and a protamine-like protein |
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