Purification and characterization of a new thiol proteinase from rat kidney - PubMed

Purification and characterization of a new thiol proteinase from rat kidney

E Gohda et al. Biochim Biophys Acta. 1981.

Abstract

The levels of activity of a new proteinase, termed cathepsin T, in rat tissues were examined. This enzyme had been previously reported to exist in rat liver on the basis of its catalysis of the conversion of multiple forms of tyrosine aminotransferase k(L-tyrosine: 2-oxoglutarate aminotransferase, EC 2.6.1.5). Kidney was found to be the richest source of cathepsin T activity, exhibiting cathepsin T activity in tissues was kidney much greater than spleen greater than liver greater than small intestine greater than lung. The proteinase activity was not detectable in heart, skeletal muscle, brain and blood. Kidney cathepsin T was purified about 1400-fold to homogeneity with a 20% yield by the purification procedure similar to that used for the liver enzyme (Gohda, E. and Pitot, H.C. (1980) J. Biol. Chem. 255, 7371-7379). Cathepsin T purified from rat kidney was found to be a glycoprotein, the molecular weight of which was between 33,500 and 35,000. Purified kidney cathepsin T converted Form I of tyrosine aminotransferase in the same way as the liver proteinase, with concomitant conversion of 52,500 dalton subunits of the aminotransferase to 48,000 dalton subunits. Kidney cathepsin T showed the same specific activities toward Form I of tyrosine aminotransferase, casein and acid-denatured hemoglobin as did the liver form of the enzyme. Many other characteristics common to the proteinases purified both from rat kidney and liver were found. We have concluded that kidney cathepsin T is the same enzyme as the liver proteinase.

Similar articles

• Purification and characterization of cathepsin J from rat liver.

  Nikawa T, Towatari T, Katunuma N. Nikawa T, et al. Eur J Biochem. 1992 Feb 15;204(1):381-93. doi: 10.1111/j.1432-1033.1992.tb16647.x. Eur J Biochem. 1992. PMID: 1740150

• Purification and tissue distribution of rat cathepsin L.

  Bando Y, Kominami E, Katunuma N. Bando Y, et al. J Biochem. 1986 Jul;100(1):35-42. doi: 10.1093/oxfordjournals.jbchem.a121703. J Biochem. 1986. PMID: 3759937

• Human cathepsin B1. Purification and some properties of the enzyme.

  Barrett AJ. Barrett AJ. Biochem J. 1973 Apr;131(4):809-22. doi: 10.1042/bj1310809. Biochem J. 1973. PMID: 4124667 Free PMC article.

• A new purification procedure of human kidney cathepsin H, its properties and kinetic data.

  Popović T, Brzin J, Kos J, Lenarcic B, Machleidt W, Ritonja A, Hanada K, Turk V. Popović T, et al. Biol Chem Hoppe Seyler. 1988 May;369 Suppl:175-83. Biol Chem Hoppe Seyler. 1988. PMID: 3202963

• Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15).

  Kirschke H, Schmidt I, Wiederanders B. Kirschke H, et al. Biochem J. 1986 Dec 1;240(2):455-9. doi: 10.1042/bj2400455. Biochem J. 1986. PMID: 3814093 Free PMC article.

Cited by

• Proteases and proteolysis in the lysosome.

  Bohley P, Seglen PO. Bohley P, et al. Experientia. 1992 Feb 15;48(2):151-7. doi: 10.1007/BF01923508. Experientia. 1992. PMID: 1740187 Review.

• Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase.

  Delaissé JM, Ledent P, Vaes G. Delaissé JM, et al. Biochem J. 1991 Oct 1;279 ( Pt 1)(Pt 1):167-74. doi: 10.1042/bj2790167. Biochem J. 1991. PMID: 1930136 Free PMC article.

• Immunological detection of a cysteine protease in the skin and other tissues.

  Fukuyama K, Ito Y, Yabe K, Epstein WL. Fukuyama K, et al. Cell Tissue Res. 1985;240(2):417-23. doi: 10.1007/BF00222354. Cell Tissue Res. 1985. PMID: 3888399

Publication types

MeSH terms

Substances