Linked Life Data

1372742

Source:http://linkedlifedata.com/resource/pubmed/id/1372742

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-4-24
pubmed:abstractText
Several proteins interact with elastin, an essential extracellular matrix element. We describe here an additional elastin-binding protein from the porcine kidney. This protein was extractable with an isotonic buffer, and was purified by a rapid and simple procedure employing its characteristic properties: high affinity for red A-agarose and spontaneous formation of cryoprecipitate. Immunohistochemical studies using antibody against the purified protein demonstrated its localization in the cytoplasm of proximal tubules of the normal rat kidney. On Western blotting using the antibody, an immunoreactive protein was detected in the liver as well as in the kidney. On the basis of the partial amino acid sequences of the purified protein, it was identified as argininosuccinate synthetase. Some biochemical properties of the protein were different from the data reporting a hepatic form of argininosuccinate synthetase, a key enzyme in the urea cycle in the liver. These results suggest that the elastin-binding property of a renal form of the enzyme may be related to a tissue-specific function in the kidney.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1011-6524
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:dateRevised
2006-8-31
pubmed:meshHeading
pubmed:articleTitle
Renal argininosuccinate synthetase: purification, immunohistochemical localization, and elastin-binding property.
pubmed:affiliation
Third Department of Internal Medicine, Akita University School of Medicine, Japan.
pubmed:publicationType
Journal Article