Abstract
Sixteen inbred or partially inbred strains of rabbits were investigated for electrophoretic and quantitative variations of alpha-1-antitrypsin (A-1-AT). We found interindividual differences in the electrophoretic A-1-AT patterns as well as quantitative differences in the concentrations of A-1-AT and the serum trypsin-inhibiting activity.
Three electrophoretic phenotypes were distinguished: M, P and MP. M was characterized by a predominant anodal A-1-AT band, and P had a major cathodal component. The MP pattern can be explained by the occurrence of the M and P components in the same serum due to heterozygosity.
The P pattern was associated with an A-1-AT concentration of approximately 56% of that in sera with the M phenotype. The levels of A-1-AT in sera with the MP phenotype were intermediate between those in M and P types.
In addition to the type-specific quantitative variation, we found a quantitative sexual dimorphism of a moderate degree: Female rabbits had A-1-AT concentrations 16% less than males.
Full Text
The Full Text of this article is available as a PDF (893.9 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Chase T., Jr, Shaw E. p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin. Biochem Biophys Res Commun. 1967 Nov 30;29(4):508–514. doi: 10.1016/0006-291x(67)90513-x. [DOI] [PubMed] [Google Scholar]
- Fagerhol M. K., Gedde-Dahl T., Jr Genetics of the Pi serum types. Family studies of the inherited variants of serum alpha-1-antitrypsin. Hum Hered. 1969;19(4):354–359. doi: 10.1159/000152238. [DOI] [PubMed] [Google Scholar]
- Ganrot P. O. Variation of the concentrations of some plasma proteins in normal adults, in pregnant women and in newborns. Scand J Clin Lab Invest Suppl. 1972;124:83–88. doi: 10.3109/00365517209102755. [DOI] [PubMed] [Google Scholar]
- Hoppe P. C., Laird C. W., Fox R. R. A simple technique for bleeding the rabbit ear vein. Lab Anim Care. 1969 Aug;19(4):524–525. [PubMed] [Google Scholar]
- James H. L., Cohen A. B. Mechanism of inhibition of porcine elastase by human alpha-1-antitrypsin. J Clin Invest. 1978 Dec;62(6):1344–1353. doi: 10.1172/JCI109255. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Koj A., Hatton M. W., Wong K. L., Regoeczi E. Isolation and partial characterization of rabbit plasma alpha1-antitrypsin. Biochem J. 1978 Mar 1;169(3):589–596. doi: 10.1042/bj1690589. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Koj A., Regoeczi E. Differential inhibition of serine proteinases by rabbit alpha 1-proteinase inhibitors F and S. Int J Pept Protein Res. 1981 Apr;17(4):519–526. doi: 10.1111/j.1399-3011.1981.tb02023.x. [DOI] [PubMed] [Google Scholar]
- Kueppers F., Mills J. Trypsin inhibition by mouse serum: sexual dimorphism controlled by testosterone. Science. 1983 Jan 14;219(4581):182–184. doi: 10.1126/science.6849130. [DOI] [PubMed] [Google Scholar]
- Morell A. G., Irvine R. A., Sternlieb I., Scheinberg I. H., Ashwell G. Physical and chemical studies on ceruloplasmin. V. Metabolic studies on sialic acid-free ceruloplasmin in vivo. J Biol Chem. 1968 Jan 10;243(1):155–159. [PubMed] [Google Scholar]