Linked Life Data

8408011

Source:http://linkedlifedata.com/resource/pubmed/id/8408011

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1993-11-18
pubmed:databankReference
pubmed:abstractText
Arginine kinase belongs to an evolutionary conserved family of ATP:guanidino phosphotransferases, whose members play an important role in energy metabolism. In this work, a lambda gt11 lobster muscle library was constructed and screened by using both polyclonal antibodies and two synthetic oligonucleotides. The complete amino acid sequence of arginine kinase (ATP:L-arginine N-phosphotransferase, EC 2.7.3.3) from lobster muscle was determined by cloning and sequencing the DNA complementary to its mRNA. The identity of the clone was confirmed by comparing the amino acid sequence deduced by nucleotide sequence analysis with previously published partial sequences of amino- and carboxyl-terminal regions of the enzyme and some of its fragments (Regnouf, F., Kassab, R., Debuire, B., Richard, C., and Han K. K. (1981) Int. J. Peptide Protein Res. 17, 143-155). The nucleotide sequence of the cDNA was found to contain an open reading frame encoding 355 amino acid residues with a calculated molecular mass of 39,830 daltons. This enzyme exhibits a significant sequence identity to those of representative members of the guanidino kinase family, including creatine kinase. This report represents the first molecular cloning and sequencing of an ATP-guanidino phosphotransferase which is not a creatine kinase isoform.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21599-605
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle.
pubmed:affiliation
Laboratoire de Biologie Structurale, UMR 9920, Centre National de la Recherche Scientifique-Université Paris-Sud, Orsay, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't