Purification and characterization of a new thiol proteinase from rat kidney.

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.