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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| Veröffentlicht in: | Archives of biochemistry and biophysics 1973-01, Vol.159 (1), p.123-133 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Sakura, J.David Timasheff, Serge N. |
| description | 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 ( |
| doi_str_mv | 10.1016/0003-9861(73)90436-0 |
| format | Article |
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| ispartof | Archives of biochemistry and biophysics, 1973-01, Vol.159 (1), p.123-133 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82193188 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 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 |
| title | Association properties of trypsin inhibitors from lima bean |
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