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Characteristics of Hiproly barley, 3: Amino acid sequences of two lysine-rich proteins [high lysine]

By: Contributor(s): Material type: ArticleArticleLanguage: En Publication details: 1980ISSN:
  • 0105-1938
Subject(s): DDC classification:
  • 81-626505
 In: Carlsberg Research Communications v. 45, no. 2, p. 79-8581-626505Summary: Two lysine-rich components isolated from 'Hiproly' barley have been subjected to sequence determination. The complete sequence of the smallest component, designated SP II B, has been determined. This protein consists of 72 amino acid residues and has a molecular weight of 8,072. The largest component, designated SP II A, was blocked to N-terminal Edman degradation, but sequence analyses of cyanogen bromide- and tryptic fragments showed that it was identical to the smallest component, except for the eight to eleven residues of which SP II A is longer in the N-terminus. Of thes residues SEVEN have been sequenced, and the following total sequence is reported
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8 ref. Summary (En)

Two lysine-rich components isolated from 'Hiproly' barley have been subjected to sequence determination. The complete sequence of the smallest component, designated SP II B, has been determined. This protein consists of 72 amino acid residues and has a molecular weight of 8,072. The largest component, designated SP II A, was blocked to N-terminal Edman degradation, but sequence analyses of cyanogen bromide- and tryptic fragments showed that it was identical to the smallest component, except for the eight to eleven residues of which SP II A is longer in the N-terminus. Of thes residues SEVEN have been sequenced, and the following total sequence is reported

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Carlsberg Lab., Copenhagen (Denmark)|COMOD

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