Conformational stability and integrity of α-amylase from mung beans: Evidence of kinetic intermediate in GdmCl-induced unfolding

Biophysical Chemistry

Volumn 137, Issue 2-3, 2008, Pages 95-99

  Tripathi, Pallavi ^a,b   Hofmann, Hagen ^b   Kayastha, Arvind M ^a   Ulbrich Hofmann, Renate ^b  

^a BANARAS HINDU UNIVERSITY   (India)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Amylase; Protein folding; Thermal transitions; Unfolding kinetics; Vigna radiata

Indexed keywords

AMYLASE; CALCIUM ION; EDETIC ACID; GUANIDINE;

ARTICLE; CIRCULAR DICHROISM; ENZYME KINETICS; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; MUNG BEAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

ALPHA-AMYLASES; CALCIUM; CIRCULAR DICHROISM; EDETIC ACID; ENZYME STABILITY; FABACEAE; GUANIDINE; HOT TEMPERATURE; KINETICS; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROPHOTOMETRY, ULTRAVIOLET; TRANSITION TEMPERATURE;

VIGNA RADIATA; VIGNA RADIATA VAR. RADIATA;

EID: 51749117809     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.07.007     Document Type: Article

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