Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-5-23
pubmed:abstractText
The relationship between two putative myosin-binding subunits of smooth muscle myosin phosphatase was investigated. A monoclonal antibody (MoAb) to the 58 kD component of smooth muscle myosin-bound phosphatase (MBP) cross-reacted with a 130 kD protein in extracts of fresh chicken gizzards. The MoAb in combination with protein A immunoprecipitated from gizzard extracts a complex of the 130 kD protein plus the 38 kD catalytic subunit of the type 1 delta protein phosphatase. It is proposed that the 130 kD component is a native subunit of MBP and that the 58 kD protein is its proteolytic degradation product. The distribution of the 130 kD component in chicken tissues was screened using the MoAb. An immunoreactive band of appropriate mass was detected in all tissues except liver and skeletal muscle. Higher concentrations of the 130 kD component were evident in the smooth muscle samples.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
429-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
A regulatory subunit of smooth muscle myosin bound phosphatase.
pubmed:affiliation
1st Department of Internal Medicine, Mie University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't