Linked Life Data

8312396

Source:http://linkedlifedata.com/resource/pubmed/id/8312396

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1994-3-23
pubmed:databankReference
pubmed:abstractText
Calpains are non-lysosomal proteases involved in myofibrillar protein degradation. To facilitate studying the expression of the porcine calpain genes and their influence on protein accretion, we have cloned partial cDNAs for mu- and m-calpain from porcine skeletal muscle via PCR amplification. A 289 bp fragment for mu-calpain and a 629 bp fragment for m-calpain were cloned into the EcoRV site of pBluescript II KS+ vector. The nucleotide sequence for porcine mu-calpain and m-calpain were 92% and 90% identical to corresponding regions of rabbit mu- and m-calpain, respectively. The deduced amino acid sequences for both mu- and m-calpain share 94% identity with respective rabbit mu- and m-calpains. Isoform specificity was validated by Southern hybridization of mu- and m-calpain probes with cloned mu- and m-calpain fragments and Northern hybridization with pig muscle mRNA. These clones will be used to evaluate the role of calpain expression in muscle hypertrophy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
931-6
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle.
pubmed:affiliation
Department of Animal Sciences, Purdue University, West Lafayette, Indiana 47907.
pubmed:publicationType
Journal Article