Electrophoretic characteristics of thermal changes of soluble proteins from several rapeseed varieties
✍ Scribed by Klepacka, M. ;Nitecka, E.
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- English
- Weight
- 107 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0027-769X
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✦ Synopsis
Poster 393 phenylalanine than those reported by these authors. WSPF and SSPF had similar amino-acid compositions except that WSPF was somewhat higher in threonine. glutamic acid. and lysine than SSPF.
Gel-filtration pattern of total proteins consisted of 3 distinct peaks (Fig. 2). The hump on the major peak suggested that it may be a mixture of more than one component. Gel-filtration pattern of crude globulin showed a peak witha prominent shoulder indicating that it wasa mixture oftwo high molecular weight components. SDS-PAGE of peak fractions confirmed this (figures not shown). SDS-PAGE also established the oligomeric nature of the major fraction as observed by other authors [I].