Crossref journal-article
Portland Press Ltd.
Biochemical Journal (288)
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.

Bibliography

Carne, A., & Moore, C. H. (1978). The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis. Biochemical Journal, 173(1), 73–83.

Authors 2
  1. A Carne (first)
  2. C H Moore (additional)
References 0 Referenced 100

None

Dates
Type When
Created 10 years ago (Aug. 10, 2015, 4:12 p.m.)
Deposited 3 years, 9 months ago (Nov. 26, 2021, 1:44 p.m.)
Indexed 2 weeks, 1 day ago (Aug. 20, 2025, 8:32 a.m.)
Issued 47 years, 2 months ago (July 1, 1978)
Published 47 years, 2 months ago (July 1, 1978)
Published Print 47 years, 2 months ago (July 1, 1978)
Funders 0

None

@article{Carne_1978, title={The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis}, volume={173}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj1730073}, DOI={10.1042/bj1730073}, number={1}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Carne, A and Moore, C H}, year={1978}, month=jul, pages={73–83} }