TY - JOUR
T1 - Natural plant enzyme inhibitors V. A trypsin/chymotrypsin inhibitor from Alocasia macrorhiza tuber
AU - Sumathi, S.
AU - Pattabiraman, T.N.
N1 - Cited By :32
Export Date: 2 March 2021
Correspondence Address: Sumathi, S.; Department of Biochemistry, Kasturba Medical College, Manipal, 576119, India
Chemicals/CAS: pepsin A, 9001-75-6; pronase, 9036-06-0; proteinase, 9001-92-7; subtilisin, 9014-01-1; trypsin inhibitor, 9035-81-8; Chymotrypsin, EC 3.4.21.1; Enzyme Inhibitors; Trinitrobenzenesulfonic Acid, 2508-19-2; Trypsin Inhibitors
Funding details: Department of Atomic Energy, Government of India, DAE
Funding text 1: This work was supported by grant B & Mc 182 from the Department of Atomic Energy, Government of India. The first author is the receipient of a Junion Research Fellowship under the above grant. The authors acknowledge the keen interest and encouragement of Dr. A. Krishna Rao, Dean, Kasturba Medical College, Manipal.
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PY - 1977
Y1 - 1977
N2 - A trypsin/chymotrypsin inhibitor was isolated from the tubers of Alocasia macrorhiza by extraction at pH 7.6, heat treatment at 80°C, ammonium sulphate precipitation and successive column chromatography on CM-cellulose, DEAE-Sephadex A-50 and Sephadex G-100. The inhibitor was pure by cellulose acetate electrophoresis. The molecular weight was approximately 32 000 as determined by gel filtration on Sephadex G-100. The inhibitor acted on bovine trypsin, human trypsin and bovine chymotrypsin. It had no action on human chymotrypsin, subtilisin BPN, pronase, Aspergillus oryzae protease, human and porcine pepsins. The bindings sites for bovine trypsin and chymotrypsin are not mutually exclusive. The inhibitor was stable over a pH range of 1-10. The purified inhibitor was far more thermostable than the crude inhibitor. The purified inhibitor lost only 33% of activity on heat treatment at 95°C for 2 h. Trinitrobenzene sulphonate treatment resulted in the loss of antichymotryptic activity faster than the antitrypsin activity of the inhibitor. © 1977.
AB - A trypsin/chymotrypsin inhibitor was isolated from the tubers of Alocasia macrorhiza by extraction at pH 7.6, heat treatment at 80°C, ammonium sulphate precipitation and successive column chromatography on CM-cellulose, DEAE-Sephadex A-50 and Sephadex G-100. The inhibitor was pure by cellulose acetate electrophoresis. The molecular weight was approximately 32 000 as determined by gel filtration on Sephadex G-100. The inhibitor acted on bovine trypsin, human trypsin and bovine chymotrypsin. It had no action on human chymotrypsin, subtilisin BPN, pronase, Aspergillus oryzae protease, human and porcine pepsins. The bindings sites for bovine trypsin and chymotrypsin are not mutually exclusive. The inhibitor was stable over a pH range of 1-10. The purified inhibitor was far more thermostable than the crude inhibitor. The purified inhibitor lost only 33% of activity on heat treatment at 95°C for 2 h. Trinitrobenzene sulphonate treatment resulted in the loss of antichymotryptic activity faster than the antitrypsin activity of the inhibitor. © 1977.
U2 - 10.1016/0005-2744(77)90204-2
DO - 10.1016/0005-2744(77)90204-2
M3 - Article
SN - 0005-2744
VL - 485
SP - 167
EP - 178
JO - BBA - Enzymology
JF - BBA - Enzymology
IS - 1
ER -