Distribution of Carboxypeptidase Isoinhibitors in the Potato Plant
Open Access
- 1 December 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 64 (6) , 1029-1031
- https://doi.org/10.1104/pp.64.6.1029
Abstract
The total amount of carboxypeptidase inhibitor was estimated in extracts of the leaves, stems, and sprouts of Solanum tuberosum L. cv. Russet Burbank. Although the tuber contained the highest levels on a dry weight basis, inhibitor was also detected in the leaves, sprouts, and upper stems. The relative amounts of each of three carboxypeptidase isoinhibitor families were estimated in several plant tissues by purifying the mixture of isoinhibitors using immobilized carboxypeptidase and then resolving the individual families by polyacrylamide gel electrophoresis. These data demonstrated both that differences in distribution are found in the potato plant and that the three isoinhibitor families described previously (Hass GM, JE Derr, DJ Makus, CA Ryan 1979 Plant Physiol 64: 1022-1028) account for essentially all of the carboxypeptidase inhibitor activity in the tissues studied.This publication has 12 references indexed in Scilit:
- Purification and Characterization of the Carboxypeptidase Isoinhibitors from PotatoesPlant Physiology, 1979
- Structure of potato carboxypeptidase inhibitor: disulfide pairing and exposure of aromatic residuesBiochemistry, 1979
- Proteinase inhibitor II from potatoes: isolation and characterization of its protomer componentsBiochemistry, 1976
- Carboxypeptidase inhibitor from potatoes. The effects of chemical modifications on inhibitory activityBiochemistry, 1976
- Amino acid sequence of a carboxypeptidase inhibitor from potatoesBiochemistry, 1975
- Purification and Properties of a Carboxypeptidase Inhibitor from PotatoesJournal of Biological Chemistry, 1974
- Chymotrypsin inhibitor I from potatoes. Large scale preparation and characterization of its subunit components.1972
- Selective enzyme purification by affinity chromatography.Proceedings of the National Academy of Sciences, 1968
- PORCINE PANCREATIC CARBOXYPEPTIDASE A SYSTEM .1. 3 FORMS OF ACTIVE ENZYME1963
- Pancreatic trypsin inhibitor. 2. Reaction with trypsinBiochemical Journal, 1953