Purification and properties of an amylase inhibitor from colocasia (Colocasia esculenta) tubers.
IR@CSIR-CFTRI
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http://ir.cftri.com/5140/
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Title |
Purification and properties of an amylase inhibitor from colocasia (Colocasia esculenta) tubers.
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Creator |
Narayana Rao, M.
Shurpalekar, K. S. Sundaravalli, O. E. |
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Subject |
05 Enzymes
23 Vegetables |
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Description |
A method for the isolation and purification of an amylase inhibitor from colocasia (Colocasia esculenta) tubers is described. The purified amylase inhibitor is a white, amorphous and hygroscopic powder containing 15.6% nitrogen. It is deficient in methionine and gives a typical protein spectrum with a maximum at 280 mg and minimum at 252 mg. The inhibitor which is electrophoretically homogeneous over a wide range of pH is stable to boiling temperatures and specifically inhibits salivary amylase. The nature of inhibition appears to be of mixed type. The activity of the inhibitor is destroyed by proteolytic enzymes, ficin and pepsin. |
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Date |
1970
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Language |
en
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Rights |
—
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Identifier |
http://ir.cftri.com/5140/1/Indian_Journal_of_Biochemistry_1970_7_241-243.pdf
Narayana Rao, M. and Shurpalekar, K. S. and Sundaravalli, O. E. (1970) Purification and properties of an amylase inhibitor from colocasia (Colocasia esculenta) tubers. Indian Journal of Biochemistry, 7. pp. 241-243. |
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