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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1982-8-26
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pubmed:abstractText |
A variant sericin polypeptide originally found by acid gel electrophoresis in the Nd-s mutant strain of the silkworm, Bombyx mori, has been analyzed genetically. The variant polypeptide (called S-2v) is encoded by a gene which behaves as a codominant allele of the gene encoding the standard S-2 sericin polypeptide. Linkage analysis locates these alleles at 0.0 map unit on chromosome 11. SDS-polyacrylamide gel electrophoresis shows that the molecular weight of the S-2v variant polypeptide is lower by approximately 62,500 than that of the S-2 polypeptide. Amino acid analysis indicates that the two sericin polypeptides have similar compositions. These results are consistent with the idea that the variant allele arose by deletion within the S-2 coding sequence in the Src-2 gene locus as the result of unequal recombination.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2928
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
165-77
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:7092799-Amino Acids,
pubmed-meshheading:7092799-Animals,
pubmed-meshheading:7092799-Bombyx,
pubmed-meshheading:7092799-Chromosome Mapping,
pubmed-meshheading:7092799-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7092799-Genes,
pubmed-meshheading:7092799-Genes, Dominant,
pubmed-meshheading:7092799-Molecular Weight,
pubmed-meshheading:7092799-Mutation,
pubmed-meshheading:7092799-Peptides, Cyclic,
pubmed-meshheading:7092799-Sericins
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pubmed:year |
1982
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pubmed:articleTitle |
Genetic variants of the Bombyx mori silkworn encoding sericin proteins of different lengths.
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pubmed:publicationType |
Journal Article
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