Abstract
Genetic variation of a codominantly inherited pancreas protease, designated CTRA-1, was discovered in the house mouse by isoelectric focusing in polyacrylamide gels. Phenotype CTRA-1A was found in MOLH/Fre and in the majority of common laboratory mouse strains. Phenotype CTRA-1B was found in PWD/Ph. It was characterized by the absence of a corresponding protease band. A third phenotype, CTRA-1C, was observed in IS/Cam and a fourth phenotype, CTRA-1D, was detected in SEG/1. CTRA-1 was found only in the pancreas and may represent the A form of chymotrypsin. The enzyme was shown to be controlled by the presumed structural locusCtra-1 located on chromosome 8. From two backcross series, including a total of 274 animals, the gene order(Es-1, Es-9)—3.9±1.7%—Got-2—3.9±1.7%—(Es-2, Es-7, Es-23)—0.7±0.5%—Ctra-1—6.3±2.2%—Prt-2 was established.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Augustinsson, K. B. (1968). The evolution of esterases in vertebrates. In van Thoai, N., and Roche, J. (eds.),Homologous Enzymes and Biochemical Evolution Gordon and Breach, New York, London, Paris, pp. 299–311.
Babson, A. L., Shapiro, P. O., Williams, P. A. R., and Phillips, G. E. (1962). The use of diazonium salt for the determination of glutamic-oxalacetic transaminase in serum.Clin. Chim. Acta 7199.
Barrett, A. (1977). Introduction to the history and classification of tissue proteinases. In Barrett, A. (ed.),Proteinases in Mammalian Cells and Tissues Elsevier/North-Holland, Amsterdam, New York, pp. 1–55.
Davisson, M., Spencer, C., Cook, S., and Akeson, E. (1989). Private communication.Mouse News Lett. 8493.
Dayhoff, M. O. (1972).Atlas of Protein Sequence and Structure, Vol. 5 Natl. Biomed. Res. Found., Washington, D.C., p. D107.
DeLorenzo, R. J., and Ruddle, F. H. (1970). Glutamate oxalate transaminase (GOT) genetics in Mus musculus: Linkage, polymorphism, and phenotypes of the Got-2 and Got-1 loci.Biochem. Genet. 4259.
Desnuelle, P. (1960). Chymotrypsin. In Boyer, Lardy, and Myrbak (eds.),The Enzymes, Vol. 4 2nd ed., Academic Press, New York, London, p. 93.
Gomori, G. (1952). Histochemistry of esterase.Int. Rev. Cytol. 1323.
Havemann, K., Gramse, M., and Gassel, W. D. (1983). Cytochemical determination of granulocyte elastase and chymotrypsin in human myeloid cells and its application in acquired deficiency states and diagnosis of myeloid leukemia.Klin. Wochenschr. 6149.
Hejgaard, J. (1981). Isoelectric focusing of subtilisin inhibitors: Detection and partial characterization of cereal inhibitors of chymotrypsin and microbial proteases.Anal. Biochem. 116444.
Honey, N. K., Sakaguchi, A. Y., Lalley, P. A., Quinto, C., MacDonald, R. J., Craik, C., Bell, G. I., Rutter, W. J., and Naylor, S. L. (1984). Chromosomal assignments of genes for trypsin, chymotrypsin B, and elastase in mouse.Somat. Cell Mol. Genet. 10377.
Kasche, V., amnéus, H., Gabel, D., and Näslund, L. (1977). Rapid zymogen activation and isolation of serine proteases from an individual mouse pancreas by affinity chromatography. Genetical heterogeneity of chymotrypsins ofMus musculus.Biochim. Biophys. Acta 4901.
Masters, C. J., and Holmes, R. S. (1975). Haemoglobin, isoenzymes and tissue differentiation. In Frontiers of Biology, vol. 42, p. 102–120, Neuberger, A., and Tatum, E. (eds.), North-Holland, Amsterdam, Oxford; American Elsevier, New York.
McGadey, J. (1967). Modified indoxyl acetate technique for the histochemical demonstration of non-specific esterases in mouse testis.J. Med. Lab. Technol. 24126.
Schaller, E., and Deimling, O. von (1979). Methionine-α-naphthyl ester, a useful chromogenic substrate for esterproteases of the mouse submandibular gland.Anal. Biochem. 93251.
Scherer, G., Bausch, E., Gaa, A., and Deimling, O. von (1989). Gene mapping on mouse chromosome 8 by interspecific crosses: New data on a linkage group conserved on human chromosome 16q1.Genomics 5275.
Schmidt, W., and Havemann, K. (1974). Isolation of elastase-like and chymotrypsin-like neutral proteases from human granulocytes.Hoppe-Seyler Z. Physiol. Chem. 3551077.
Shaw, E., Mares-Guia, M., and Cohen, W. (1965). Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-lysine.Biochemistry 42219.
Starkey, P. M., and Barrett, A. J. (1976). Neutral proteinases of human spleen. Purification and criteria for homogeneity of elastase and cathepsin G.Biochem. J. 155255.
Takuma, T., and Kumegawa, M. (1981). Independent inductions of trypsin-like esteroproteases by 5α-dihydrotestosterone and triiodothyronine in mouse submandibular gland.J. Biochem. 901371.
Watanabe, T., and Tomita, T. (1974). Genetic study of pancreatic proteinase and α-amylase in mice (Mus musculus).Biochem. Genet. 12419.
Watanabe, T., Ogasawara, N., and Goto, H. (1976a). Genetic study of pancreatic proteinase in mice (Mus musculus): Genetic variants of trypsin and chymotrypsin.Biochem. Genet. 14697.
Watanabe, T., Ogasawara, N., and Goto, H. (1976b). Genetic study of pancreatic proteinase in mice (Mus musculus): Linkage of the Prt-2 locus on chromosome 8.Biochem. Genet. 14999.
Watanabe, T., Ito, T., and Ogasawara, N. (1982). Biochemical markers of three strains derived from Japanese wild mouse (Mus musculus molossinus).Biochem. Genet. 20385.
Watanabe, T., Miyashita, N., Moriwaki, K., and Hilgers, J. (1987). Evolutionary relationships between laboratory mice and subspecies of Mus musculus based on the genetic study of pancreatic proteinase loci, Prt-1, Prt-2, Prt-3, and Prt-6.Biochem. Genet. 2523.
Author information
Authors and Affiliations
Additional information
This work was supported by the Deutsche Forschungsgemeinschaft, De 315/4.
Rights and permissions
About this article
Cite this article
von Deimling, O.H., Gröning, J. & Gaa, A. Genetic and biochemical characterization of a new chymotrypsin isozyme of the house mouse, CTRA-1. Biochem Genet 29, 545–557 (1991). https://doi.org/10.1007/PL00020697
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/PL00020697