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PMID: 3017764 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence.

FEBS letters ·Vol. 205 ·No. 2 ·1986-09-15 ·Pages 313-7

Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K

Abstract

The complete amino acid sequence of the large subunit (catalytic subunit) of human low-Ca2+-requiring-calcium-activated neutral protease (muCANP) was deduced from its cDNA base sequence. It is composed of 714 amino acid residues and its sequence is highly homologous to the chicken CANP sequence determined previously. Human muCANP, like chicken CANP, has a clear 4-domain structure, and their fundamental structures are essentially the same, although their Ca2+ sensitivities are significantly different. The role of each domain in the Ca2+ sensitivity and protease activity of CANP is discussed on the basis of sequence comparison.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Calpain/genetics Chickens/genetics DNA/genetics Enzyme Activation/drug effects Humans Peptide Hydrolases Sequence Homology, Nucleic Acid
Chemicals
DNA Peptide Hydrolases Calpain
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Aoki K
Imajoh S
Ohno S
Emori Y
Koike M
Kosaki G
Suzuki K
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1986-09-15
Pages
313-7
Language
English
Region
England
NLM ID
0155157
Subset
IM
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