Abstract
During our human heart cDNA sequencing project, we have obtained a novel cDNA clone which is very similar in DNA and amino acid sequences to a rat/mouse cysteine-rich intestinal protein (1). Sequence analysis has shown that this human cysteine-rich heart protein (hCRHP) is a protein of 77 amino acids and possesses a LIM motif which is considered to be able to bind zinc. Northern blot analyses have shown that its mRNA level in rat heart is regulated developmentally. We have expressed hCRHP in E. coli using pAED4 as the vector and the cDNA was engineered so that the authentic protein is produced. The protein was partially purified and was shown to be a basic protein.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adult
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Blotting, Northern
-
Carrier Proteins / genetics
-
Carrier Proteins / metabolism
-
DNA, Complementary
-
Escherichia coli / genetics
-
Gene Expression Regulation, Developmental*
-
Heart / growth & development
-
Humans
-
LIM Domain Proteins
-
Molecular Sequence Data
-
Myocardium / metabolism*
-
Nuclear Proteins*
-
Proteins*
-
Proto-Oncogene Proteins c-myc / genetics*
-
Rats
-
Sequence Homology, Amino Acid
-
Zinc / metabolism
-
Zinc Fingers*
Substances
-
CRIP1 protein, human
-
Carrier Proteins
-
Crip1 protein, mouse
-
Crip1 protein, rat
-
DNA, Complementary
-
LIM Domain Proteins
-
Nuclear Proteins
-
Proteins
-
Proto-Oncogene Proteins c-myc
-
cysteine-rich protein, mammalian
-
Zinc