Previously we reported the amino acid sequences of 4 well-defined sacroplasmic, high-affinity Ca(2+)-binding proteins in the protochordate amphioxus, Branchiostoma lanceolatum [1]. Here we report on the complete amino acid sequence determination of 3 additional minor isoforms. The seven isoforms differ from each other in 9 positions of a contiguous 17-residue-long segment (positions 20-36) and can be classified in a alpha (ASCP I, III and IV) and a beta lineage (ASCP II, V, VI and VII).
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Previously we reported the amino acid sequences of 4 well-defined sacroplasmic, high-affinity Ca(2+)-binding proteins in the protochordate amphioxus, Branchiostoma lanceolatum [1]. Here we report on the complete amino acid sequence determination of 3 additional minor isoforms. The seven isoforms differ from each other in 9 positions of a contiguous 17-residue-long segment (positions 20-36) and can be classified in a alpha (ASCP I, III and IV) and a beta lineage (ASCP II, V, VI and VII).
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| uniprot:name |
FEBS Lett.
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| uniprot:author |
Cox J.A.,
Takagi T.,
Valette-Talbi L.
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| uniprot:date |
1992
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| uniprot:pages |
159-160
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| uniprot:title |
Primary structure of three minor isoforms of amphioxus sarcoplasmic calcium-binding proteins.
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| uniprot:volume |
302
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| dc-term:identifier |
doi:10.1016/0014-5793(92)80429-K
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