Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have isolated the bovine COX8H gene for the heart/muscle isoform of cytochrome c oxidase (COX) subunit VIII from a library of bovine genomic DNA cloned into lambda EMBL3. Primer extension assays on bovine heart mRNA mapped the 5' ends of COX8H transcripts to a CA dinucleotide 62-bp upstream from the ATG codon. The gene thus spans 1565-bp and comprises two exons and one large intron of 1227 bp. Exon 1 encodes the 5' untranslated region, a 24-amino acid presequence, and the first 13 amino acids of the mature COX VIII-H protein. Exon 2 encodes the remainder of the cDNA: amino acids 14 to 46 plus the 66-bp 3' untranslated region. The exon-intron boundaries matched the consensus splice junction sequences. Two protein polymorphisms were seen: an Ala/Val polymorphism at position -6 in the presequence and the previously noted Lys/Arg polymorphism at residue 7 of the mature protein. A TaqI polymorphism occurs in the intron. The COX8H gene was mapped by bovine x rodent somatic cell hybrid mapping panels to bovine (BTA) Chromosome (Chr) 25 with 100% concordancy. BTA 25 is conserved relative to the long arm of human (HSA) Chr 11, which contains COX8, the gene for the single human COX VIII subunit that is homologous to the liver isoform.
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PMID:Structure and chromosomal location of the bovine gene for the heart muscle isoform of cytochrome c oxidase subunit VIII. 776 94

Previous studies of hemoglobin-based oxygen carriers and their effects on coagulation have shown conflicting results. This study re-examined the effect of hemoglobin solution on blood coagulation in whole blood using highly purified human hemoglobin Ao (HbAo). Citrated human whole blood samples were diluted 1:1 with HbAo (7gHb/dl) or human serum albumin (HSA; 5g/dl) as a protein control, and both activated partial thromboplastin time (aPTT) and prothrombin time (PT) were measured using a mechanically based whole blood coagulometer. Multiple runs were performed with the same volunteer donor sample. The mean aPTT time of HbAo-diluted samples (105.9 +/- 19.9 sec., n = 41) was significantly longer than the undiluted controls (46.4 +/- 5.6 sec., n = 54) or HSA-diluted blood (77.1 +/- 12.7 sec., n = 41) indicating an abnormal intrinsic coagulation pathway. There was no significant difference between the PT times of the HbAo and HSA-diluted samples. To examine the cause of the prolonged aPTT times with HbAo dilution, we performed activity assays of intrinsic factors XII, XI, IX, and VIII in a citrated human whole blood system diluted 1/5 and 1/10 with normal saline solution (NSS), and then 1:1 with either HbAo, HSA, or NSS. Only the Factor IX activity was significantly depressed by hemodilution (1/5 HbAo 50.20 +/- 8.11; HSA 61.05 +/- 6.72; NSS 74.75 +/- 9.83. 1/10 HbAo 46.50 +/- 5.57; HSA 64.97 +/- 11.01; NSS 67.92 +/- 16.03). These results suggest that in-vitro hemodilution with HbAo causes a hypocoagulatory response through interference with Factor IX function.
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PMID:Decreased whole blood factor IX activity following hemodilution with hemoglobin A-zero in-vitro. 916 43