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PMID: 687380 Published · ppublish English Journal Article

The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis.

The Biochemical journal ·Vol. 173 ·No. 1 ·1978-07-01 ·Pages 73-83

Carne A, Moore CH

Abstract

The amino acid sequences of the tryptic peptides of the thiol proteinase actinidin from Actinidia chinensis were determined by the manual dansyl--Edman procedure. There are 12 tryptic peptides, which give a polypeptide chain of 220 residues with a mol.wt. of 23500. An alignment of the tryptic peptides was made by using the X-ray-crystallographic data of Baker [(1977) J. Mol. Biol. 115, 263--277] determined at 0.28 nm resolution on crystalline actinidin. Detailed evidence for the amino acid sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50083 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

MeSH Terms
Amino Acid Sequence Chemical Phenomena Chemistry Chromatography, DEAE-Cellulose Chromatography, Gel Cysteine Endopeptidases Endopeptidases/isolation & purification Peptide Fragments/isolation & purification Plants/enzymology Trypsin
Chemicals
Peptide Fragments Endopeptidases Trypsin Cysteine Endopeptidases actinidain
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Carne A
Moore C H
References (27)
27 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1730073
Published
1978-07-01
Pages
73-83
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1185751
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1730073 PMC Full Text View journal details
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