Abstract
The A 5 subunit of the glycinin seed storage protein of soybean was purified by ion‐exchange chromatography followed by preparative SDS‐gel electrophoresis and the complete amino acid sequence was determined. The A 5 subunit is composed of 97 amino acids which correspond to an M r of ~10600. Approx. 86% of the sequence of the A 5 subunit was found to be identical to that of the NH 2 ‐terminal region of the A 3 subunit of the glycinin determined previously. Also, the A 4 subunit of the glycinin was purified and the partial sequence was determined. The sequence of the A 4 subunit was estimated to be highly homologous to that of the COOH‐terminal region of the A 3 subunit.
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Claims 4
Claim · model-written summary
The soybean glycinin A5 subunit has 97 amino acids.
Not reportedTaxon
Verbatim
e0“The A 5 subunit is composed of 97 amino acids”
Claim · model-written summary
The A5 subunit corresponds to an approximate molecular mass of 10600.
Not reportedTaxon
Verbatim
e0“which correspond to an M r of ~10600”
Claim · model-written summary
About 86% of A5 sequence is identical to the previously determined N-terminal A3 region.
Not reportedTaxon
Verbatim
e0“Approx. 86% of the sequence of the A 5 subunit was found to be identical to that of the NH 2 ‐terminal region of the A 3 subunit of the glycinin determined previously”
Claim · model-written summary
The A4 subunit was highly homologous to the C-terminal region of A3.
Not reportedTaxon
Verbatim
e0“The sequence of the A 4 subunit was estimated to be highly homologous to that of the COOH‐terminal region of the A 3 subunit”