Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences.

Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Research Abstract Details 

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Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Abstract Text:

K Nakano,T Fukui,H Matsubara,

To elucidate the structural similarity between alpha-glucan phosphorylases from different sources, the amino acid sequences of the cysteinyl regions in potato phosphorylase were determined, and compared with the complete sequence of the rabbit muscle enzyme. Cysteinyl peptides were purified by covalent chromatography based on thiol-disulfide exchange. Potato phosphorylase was coupled to Thiopropyl-Sepharose 6B in the presence of urea, and, after tryptic digestion, 10 distinct cysteinyl peptides which accounted for all the cysteine present in the enzyme were finally isolated in high yields. From the sequence comparison, all of the peptides surrounding the cysteinyl residues in the potato enzyme are homologous with widely distributed specific regions in the rabbit muscle enzyme, although only 4 of 10 cysteinyl residues are conserved between the two enzymes. These observations, in addition to the previously established homology in the cofactor site, show that potato and rabbit muscle phosphorylases are similar in terms of the primary structure. The different properties of cysteinyl residues in the two enzymes are discussed based on the present sequence comparison and the recent X-ray crystallographic data for the rabbit muscle enzyme.

Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Publishing Authors By Initials

K Nakano,T Fukui,H Matsubara,

For similar biological phenomena, cell phenomena, and immunity: immunity: antibody specificity: species specificity research abstracts see: biological phenomena, cell phenomena, and immunity: immunity: antibody specificity: species specificity research

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Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 87

Page Numbers: 919-27

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Mar

YEAR: 1980

Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Keywords Mesh Terms:

KEYWORDS: Species Specificity

MESH TERMS: enzymology

Chemical & Substance for Abstract: Sequence homology between potato and rabbit muscle phosphroylases. Isolation of cysteinyl peptides by covalent chromatography from the potato enzyme and their amino acid sequences. Information

Substance Name: Phosphorylases

Registry Number: EC 2.4.1.-

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Country: JAPAN

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MEDLINETA: J Biochem

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