The subunit structure of alpha-crystallin. Isolation and characterization of the S-carboxymethylated acidic subunits from adult and embryonic origin
The present results, together with physicochemical evidence presented elsewhere, indicate that α‐crystallin from calf lens is composed of two acidic and two basic polypeptide chains. The acidic polypeptides could be isolated by chromatography on SE‐Sephadex at pH 5.5 in the presence of 7 M urea. It...
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| Veröffentlicht in: | European journal of biochemistry 1969-12, Vol.11 (3), p.472-481 |
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| container_title | European journal of biochemistry |
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| creator | Schoenmakers, J G Gerding, J J Bloemendal, H |
| description | The present results, together with physicochemical evidence presented elsewhere, indicate that α‐crystallin from calf lens is composed of two acidic and two basic polypeptide chains. The acidic polypeptides could be isolated by chromatography on SE‐Sephadex at pH 5.5 in the presence of 7 M urea. It could be demonstrated that both
S
‐carboxymethylated acidic polypeptides are of equal molecular weight and amino acid composition. In both chains
N
‐acetylmethionyl‐aspartate was found as the N‐terminal and serine as the C‐terminal residue. Peptide mapping reveals one unique peptide region for each polypeptide.
In embryonic α‐crystallin only one acidic polypeptide can be detected. From comparative amino acid analysis, peptide maps as well as physicochemical behaviour it may be deduced that the polypeptide present in the early embryonic stages is identical with the adult acidic polypeptide A‐2. |
| doi_str_mv | 10.1111/j.1432-1033.1969.tb00797.x |
| format | Article |
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S
‐carboxymethylated acidic polypeptides are of equal molecular weight and amino acid composition. In both chains
N
‐acetylmethionyl‐aspartate was found as the N‐terminal and serine as the C‐terminal residue. Peptide mapping reveals one unique peptide region for each polypeptide.
In embryonic α‐crystallin only one acidic polypeptide can be detected. From comparative amino acid analysis, peptide maps as well as physicochemical behaviour it may be deduced that the polypeptide present in the early embryonic stages is identical with the adult acidic polypeptide A‐2.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1969.tb00797.x</identifier><identifier>PMID: 4983849</identifier><language>eng</language><publisher>England</publisher><subject>Aging ; Alkylation ; Amino Acids - analysis ; Animals ; Aspartic Acid - analysis ; Carbon Isotopes ; Cattle ; Chromatography, Ion Exchange ; Crystallins - analysis ; Electrophoresis ; Gels ; Immunodiffusion ; Lens, Crystalline - embryology ; Methionine - analysis ; Molecular Weight ; Peptides - analysis ; Rabbits ; Serine - analysis ; Sulfhydryl Compounds - analysis ; Ultracentrifugation ; Urea</subject><ispartof>European journal of biochemistry, 1969-12, Vol.11 (3), p.472-481</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c257t-80ced6f2928499ecdb361ad4753d8fc729191df1fc76ee0528270bf8b494e3c43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4983849$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schoenmakers, J G</creatorcontrib><creatorcontrib>Gerding, J J</creatorcontrib><creatorcontrib>Bloemendal, H</creatorcontrib><title>The subunit structure of alpha-crystallin. Isolation and characterization of the S-carboxymethylated acidic subunits from adult and embryonic origin</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The present results, together with physicochemical evidence presented elsewhere, indicate that α‐crystallin from calf lens is composed of two acidic and two basic polypeptide chains. The acidic polypeptides could be isolated by chromatography on SE‐Sephadex at pH 5.5 in the presence of 7 M urea. It could be demonstrated that both
S
‐carboxymethylated acidic polypeptides are of equal molecular weight and amino acid composition. In both chains
N
‐acetylmethionyl‐aspartate was found as the N‐terminal and serine as the C‐terminal residue. Peptide mapping reveals one unique peptide region for each polypeptide.
In embryonic α‐crystallin only one acidic polypeptide can be detected. From comparative amino acid analysis, peptide maps as well as physicochemical behaviour it may be deduced that the polypeptide present in the early embryonic stages is identical with the adult acidic polypeptide A‐2.</description><subject>Aging</subject><subject>Alkylation</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Aspartic Acid - analysis</subject><subject>Carbon Isotopes</subject><subject>Cattle</subject><subject>Chromatography, Ion Exchange</subject><subject>Crystallins - analysis</subject><subject>Electrophoresis</subject><subject>Gels</subject><subject>Immunodiffusion</subject><subject>Lens, Crystalline - embryology</subject><subject>Methionine - analysis</subject><subject>Molecular Weight</subject><subject>Peptides - analysis</subject><subject>Rabbits</subject><subject>Serine - analysis</subject><subject>Sulfhydryl Compounds - analysis</subject><subject>Ultracentrifugation</subject><subject>Urea</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1969</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9UU1v2zAMFYYNXdrtJwwQdtjNrr5iS7sNRdcWKNBDu7MgS_SiwLYySQbi_o7-4ClNWl5IkO89gnwIfaekpiUutzUVnFWUcF5T1ag6d4S0qq33H9DqffQRrQihomJq3XxG5yltCSGNatozdCaU5FKoFXp52gBOczdPPuOU42zzHAGHHpthtzGVjUvKZhj8VOO7FAaTfZiwmRy2GxONzRD987FZOLmIPVbWxC7slxHyZikEcNhY77x925NwH8OIjZuH_CoFYxeXMBVEiP6vn76gT70ZEnw95Qv05_f109Vtdf9wc3f1676ybN3mShILrumZYuUUBdZ1vKHGiXbNnextyxRV1PW0lA0AWTPJWtL1shNKALeCX6AfR91dDP9mSFmPPlkYBjNBmJOWgjdSclaAP49AG0NKEXq9i340cdGU6IMleqsPf9eHv-uDJfpkid4X8rfTlrkbwb1TTx7w_yqHjW4</recordid><startdate>196912</startdate><enddate>196912</enddate><creator>Schoenmakers, J G</creator><creator>Gerding, J J</creator><creator>Bloemendal, H</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>7X8</scope></search><sort><creationdate>196912</creationdate><title>The subunit structure of alpha-crystallin. Isolation and characterization of the S-carboxymethylated acidic subunits from adult and embryonic origin</title><author>Schoenmakers, J G ; Gerding, J J ; Bloemendal, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c257t-80ced6f2928499ecdb361ad4753d8fc729191df1fc76ee0528270bf8b494e3c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1969</creationdate><topic>Aging</topic><topic>Alkylation</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Aspartic Acid - analysis</topic><topic>Carbon Isotopes</topic><topic>Cattle</topic><topic>Chromatography, Ion Exchange</topic><topic>Crystallins - analysis</topic><topic>Electrophoresis</topic><topic>Gels</topic><topic>Immunodiffusion</topic><topic>Lens, Crystalline - embryology</topic><topic>Methionine - analysis</topic><topic>Molecular Weight</topic><topic>Peptides - analysis</topic><topic>Rabbits</topic><topic>Serine - analysis</topic><topic>Sulfhydryl Compounds - analysis</topic><topic>Ultracentrifugation</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schoenmakers, J G</creatorcontrib><creatorcontrib>Gerding, J J</creatorcontrib><creatorcontrib>Bloemendal, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schoenmakers, J G</au><au>Gerding, J J</au><au>Bloemendal, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The subunit structure of alpha-crystallin. Isolation and characterization of the S-carboxymethylated acidic subunits from adult and embryonic origin</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1969-12</date><risdate>1969</risdate><volume>11</volume><issue>3</issue><spage>472</spage><epage>481</epage><pages>472-481</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The present results, together with physicochemical evidence presented elsewhere, indicate that α‐crystallin from calf lens is composed of two acidic and two basic polypeptide chains. The acidic polypeptides could be isolated by chromatography on SE‐Sephadex at pH 5.5 in the presence of 7 M urea. It could be demonstrated that both
S
‐carboxymethylated acidic polypeptides are of equal molecular weight and amino acid composition. In both chains
N
‐acetylmethionyl‐aspartate was found as the N‐terminal and serine as the C‐terminal residue. Peptide mapping reveals one unique peptide region for each polypeptide.
In embryonic α‐crystallin only one acidic polypeptide can be detected. From comparative amino acid analysis, peptide maps as well as physicochemical behaviour it may be deduced that the polypeptide present in the early embryonic stages is identical with the adult acidic polypeptide A‐2.</abstract><cop>England</cop><pmid>4983849</pmid><doi>10.1111/j.1432-1033.1969.tb00797.x</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1969-12, Vol.11 (3), p.472-481 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84368832 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Aging Alkylation Amino Acids - analysis Animals Aspartic Acid - analysis Carbon Isotopes Cattle Chromatography, Ion Exchange Crystallins - analysis Electrophoresis Gels Immunodiffusion Lens, Crystalline - embryology Methionine - analysis Molecular Weight Peptides - analysis Rabbits Serine - analysis Sulfhydryl Compounds - analysis Ultracentrifugation Urea |
| title | The subunit structure of alpha-crystallin. Isolation and characterization of the S-carboxymethylated acidic subunits from adult and embryonic origin |
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