Association properties of trypsin inhibitors from lima bean

The molecular-weight properties of three purified proteinase inhibitors from lima bean were studied by using high speed sedimentation equilibrium. Two isoinhibitors [fraction I and II, nomenclature from Jones et al., (18)]do not self-associate at moderate pH and concentration (

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Bibliographische Detailangaben
Veröffentlicht in:	Archives of biochemistry and biophysics 1973-01, Vol.159 (1), p.123-133
Hauptverfasser:	Sakura, J.David, Timasheff, Serge N.
Format:	Artikel
Sprache:	eng
Schlagworte:	Dialysis horticultural crops Hydrogen-Ion Concentration Kinetics Macromolecular Substances Mathematics Molecular Weight plant biochemistry plant physiology Plant Proteins - analysis Plants - analysis Protein Binding Spectrophotometry, Ultraviolet Thermodynamics Trypsin Inhibitors - analysis Ultracentrifugation
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Beschreibung
Zusammenfassung:	The molecular-weight properties of three purified proteinase inhibitors from lima bean were studied by using high speed sedimentation equilibrium. Two isoinhibitors [fraction I and II, nomenclature from Jones et al., (18)]do not self-associate at moderate pH and concentration (
ISSN:	0003-9861 1096-0384
DOI:	10.1016/0003-9861(73)90436-0