doi: 10.1104/pp.66.5.838.
Microheterogeneity of globulin-1 storage protein from French bean with isoelectrofocusing
Affiliations
- PMID: 16661537
- PMCID: PMC440737
- DOI: 10.1104/pp.66.5.838
Item in Clipboard
Microheterogeneity of globulin-1 storage protein from French bean with isoelectrofocusing
Plant Physiol.
1980 Nov.
Abstract
The major storage protein fraction, globulin-1 protein, of French bean (Phaseolus vulgaris L.) was analyzed by two-dimensional electrophoresis. The protein pattern suggested a more complex system for globulin-1 protein than the model of three polypeptides, alpha, beta, and gamma, differing in molecular weight. Isoelectrofocusing analyses of the individual proteins showed that each exhibited charge microheterogeneity over a similar pH range. Isoelectrofocusing banding patterns may help to understand the relationships between the globulin-1 polypeptide subunits.
Similar articles
-
Genetic variation in the subunits of globulin-1 storage protein of French bean.Theor Appl Genet. 1981 Mar;59(2):83-8. doi: 10.1007/BF00285895. Theor Appl Genet. 1981. PMID: 24276385
-
Equal Expression of the Maternal and Paternal Alleles for the Polypeptide Subunits of the Major Storage Protein of the Bean Phaseolus vulgaris L.Plant Physiol. 1977 Jun;59(6):1122-4. doi: 10.1104/pp.59.6.1122. Plant Physiol. 1977. PMID: 16660005 Free PMC article.
-
Heritable Variation in a Polypeptide Subunit of the Major Storage Protein of the Bean, Phaseolus vulgaris L.Plant Physiol. 1975 Dec;56(6):776-9. doi: 10.1104/pp.56.6.776. Plant Physiol. 1975. PMID: 16659393 Free PMC article.
-
Cell-free Synthesis of the Major Storage Protein of the Bean, Phaseolus vulgaris L.Plant Physiol. 1975 Dec;56(6):780-5. doi: 10.1104/pp.56.6.780. Plant Physiol. 1975. PMID: 16659394 Free PMC article.
-
Molecular size, subunit structure and microheterogeneity of glycoprotein II from the seeds of kidney bean (Phaseolus vulgaris L.).Biochim Biophys Acta. 1980 Jun 26;623(2):418-28. doi: 10.1016/0005-2795(80)90271-8. Biochim Biophys Acta. 1980. PMID: 7397224
Cited by
-
Contribution of processing events to the molecular heterogeneity of four banding types of phaseolin, the major storage protein of Phaseolus vulgaris L.Plant Mol Biol. 1984 Nov;3(6):345-53. doi: 10.1007/BF00033381. Plant Mol Biol. 1984. PMID: 24310567
-
Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons.J Cell Biol. 1982 May;93(2):306-13. doi: 10.1083/jcb.93.2.306. J Cell Biol. 1982. PMID: 7096441 Free PMC article.
-
Linkage relationships between genes controlling seed proteins in French bean.Theor Appl Genet. 1981 Oct;60(4):251-9. doi: 10.1007/BF02342545. Theor Appl Genet. 1981. PMID: 24276741
-
In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum: evidence for two glycosylation steps.J Cell Biol. 1983 Apr;96(4):999-1007. doi: 10.1083/jcb.96.4.999. J Cell Biol. 1983. PMID: 6833399 Free PMC article.
-
An analysis of the subunit structure of the crystalloid protein complex from castor bean endosperm.Plant Physiol. 1983 Jun;72(2):376-81. doi: 10.1104/pp.72.2.376. Plant Physiol. 1983. PMID: 16663009 Free PMC article.
References
LinkOut - more resources
Full Text Sources
