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Prevalence and inheritance of factor XI (plasma thromboplastin antecedent) deficiency in cattle.

A survey of 169 Holstein-Friesian cattle showed 21 heterozygous for Factor XI activity having activities of .43 +/- .10 units per milliliter compared with the normal .99 +/- .32 units per milliliter. The frequency of the mutant gene was .06; the 95% confidence limits for the frequency of homozygotes in the population were .1 to .8%, and for heterozygotes the frequency was 7.0 to 16.0%. Test matings indicated this disorder is transmitted as an autosomal recessive gene.

Animals↗

The hydrolysis of biologically active peptides by bovine lung tissue factor (thromboplastin).

Tissue factor apoprotein and relipidated tissue factor preparations extensively hydrolyze bradykinin, Lys-bradykinin, Met-Lys-bradykinin, substance P, [Asp1, Ile5]-angiotensin II, [Asp1, Ile5]-angiotensin I, and human fibrinopeptide A while acting more slowly on [Sar1, Ile5]-angiotensin II, [Me2Gly1, Ile5]-angiotensin II, bradykinin potentiating pentapeptide from B. jararaca, luteinizing hormone-releasing hormone, melanocyte stimulating hormone-release-inhibiting factor (Pro-Leu-Gly-NH2), and oxytocin. No hydrolysis of thyrotropin-releasing factor or bradykinin potentiating nonapeptide from B. jararaca is observed. Relipidated and apoprotein tissue factor act at identical rates under the conditions of the assay. Dansylation and chromatography of tissue factor-peptide incubation mixtures further indicate that relipidated and apoprotein tissue factor also hydrolyze peptides by identical mechanisms. No fewer than six bonds are hydrolyzed in bradykinin while the angiotensins and substance P are degraded to constituent amino acids. Only the N-terminal alanine is released from fibrinopeptide A. 2-Mercaptoethanol greatly inhibits the hydrolysis of bradykinin by relipidated tissue factor.

Angiotensin II↗