Linked Life Data

10704658

Source:http://linkedlifedata.com/resource/pubmed/id/10704658

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2000-4-11
pubmed:abstractText
The expression of high-molecular-weight and low-molecular-weight kininogen mRNAs in the whale liver was examined by reverse transcription-polymerase chain reaction. The nucleotide sequences of the high-molecular-weight and low-molecular-weight kininogen cDNAs were analyzed and deduced to the amino acid sequences. The high-molecular-weight kininogen composed of 609 amino acid residues with 18 signal peptides possessed the consensus sequences of the cysteine protease inhibitor domains I and II, the bradykinin domain, the histidine-rich region, and the prekallikrein-binding region. Except for the histidine-rich region, the overall homologies with bovine, human, and rat high-molecular-weight kininogens were 81%, 76%, and 62%, respectively. The low-molecular-weight kininogen is composed of 408 amino acid residues. The nucleotide sequence down to C(1200) as well as the amino acid sequence till Ile(382) is identical to that of the high-molecular-weight kininogen. The remaining low-molecular-weight kininogen-specific carboxy-terminal portion possessed an amino acid sequence similar to that of the land mammals. The overall homologies with bovine, human, and rat low-molecular-weight kininogens were 82%, 79%, and 64%, respectively. The amino acid sequences of both whale high-molecular-weight and low-molecular-weight kininogens are most similar to those of the bovine among the land mammals analyzed so far. An incubation of dolphin/whale plasma with human plasma kallikrein, or with bovine trypsin, in the presence of carboxypeptidase inhibitors generated bradykinin antigen as well as the spasmogenic activity to the estrous rat uterus. The amount of bradykinin released by the latter enzyme was almost double of the former, indicating that the dolphin/whale plasma contained similar concentrations of low-molecular-weight and high-molecular-weight kininogens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
481-90
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed-meshheading:10704658-Amino Acid Sequence, pubmed-meshheading:10704658-Animals, pubmed-meshheading:10704658-Base Sequence, pubmed-meshheading:10704658-Bradykinin, pubmed-meshheading:10704658-Cattle, pubmed-meshheading:10704658-DNA, Complementary, pubmed-meshheading:10704658-Dolphins, pubmed-meshheading:10704658-Factor XI, pubmed-meshheading:10704658-Humans, pubmed-meshheading:10704658-Kallikreins, pubmed-meshheading:10704658-Kininogen, High-Molecular-Weight, pubmed-meshheading:10704658-Kininogen, Low-Molecular-Weight, pubmed-meshheading:10704658-Molecular Sequence Data, pubmed-meshheading:10704658-Prekallikrein, pubmed-meshheading:10704658-Protein Structure, Tertiary, pubmed-meshheading:10704658-Rats, pubmed-meshheading:10704658-Sequence Alignment, pubmed-meshheading:10704658-Sequence Analysis, DNA, pubmed-meshheading:10704658-Sequence Homology, Amino Acid, pubmed-meshheading:10704658-Trypsin, pubmed-meshheading:10704658-Whales
pubmed:year
2000
pubmed:articleTitle
Whale high-molecular-weight and low-molecular-weight kininogens.
pubmed:affiliation
Department of Laboratory Medicine, School of Medicine, Kumamoto, Japan.
pubmed:publicationType
Journal Article