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PMID: 3541893 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular cloning of two cysteine proteinases from paw-paw (Carica papaya).

The Biochemical journal ·Vol. 237 ·No. 1 ·1986-07-01 ·Pages 105-10

McKee RA, Adams S, Matthews JA, Smith CJ, Smith H

Abstract

Two cDNA clones for plant cysteine proteinases have been isolated from a Carica papaya (paw-paw, papaya) leaf tissue cDNA library by using a mixture of 16 synthetic oligodeoxyribonucleotides as a hybridization probe. The inserted regions are 311 and 440 base-pairs in length and have the potential to encode a region corresponding to the C-terminal region of two proteins which are homologous with the known plant cysteine proteinases and the mammalian thiol cathepsins. One of the sequences shows a high (greater than 77%) homology with the plant cysteine proteinase papain, the other is closely related to papaya chymopapain. One sequence contains all, and the other most, of the 3' untranslated region of the mRNA. The inserts were used as specific probes in Northern Blot analyses giving an estimated size for the two mRNA species of 1.45 kilobases.

MeSH Terms
Amino Acid Sequence Base Sequence Cloning, Molecular Cysteine Endopeptidases DNA Endopeptidases/genetics Isoenzymes/genetics Nucleic Acid Hybridization Plants/enzymology,genetics RNA, Messenger/genetics
Chemicals
Isoenzymes RNA, Messenger DNA Endopeptidases Cysteine Endopeptidases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
McKee R A
Adams S
Matthews J A
Smith C J
Smith H
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28 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1986-07-01
Pages
105-10
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1146953
Subset
IM
Databases
GENBANK
M24252
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