More stable structure of wheat germ lipase at low pH than its native state

Biochimie

Volumn 92, Issue 7, 2010, Pages 885-893

  Ahmad, Ejaz ^a   Fatima, Sadaf ^a   Khan, Mohd Moin ^a   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Acid induced state; Enzyme activity; Molten globule; PH induced denaturation; Wheat germ lipase

Indexed keywords

TRIACYLGLYCEROL LIPASE; ACRYLAMIDE; GUANIDINE; NAPHTHALENESULFONIC ACID DERIVATIVE; PROTEIN SUBUNIT;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; LIGHT SCATTERING; MOLECULAR WEIGHT; NONHUMAN; PH; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; WHEAT GERM; CHEMISTRY; DRUG EFFECTS; ENZYMOLOGY; METABOLISM; PROTEIN DENATURATION; PROTEIN SUBUNIT; SPECTROFLUOROMETRY; TEMPERATURE; WHEAT;

ACRYLAMIDE; CIRCULAR DICHROISM; ENZYME STABILITY; GUANIDINE; HYDROGEN-ION CONCENTRATION; LIPASE; MOLECULAR WEIGHT; NAPHTHALENESULFONATES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TRITICUM;

EID: 77953543617     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.03.023     Document Type: Article

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