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Sun SM, Mutschler MA, Bliss FA, et al. Protein Synthesis and Accumulation in Bean Cotyledons during Growth. Plant Physiol. 1978;61(6):918-23doi: 10.1104/pp.61.6.918.
Sun, S. M., Mutschler, M. A., Bliss, F. A., & Hall, T. C. (1978). Protein Synthesis and Accumulation in Bean Cotyledons during Growth. Plant physiology, 61(6), 918-23. https://doi.org/10.1104/pp.61.6.918
Sun, S M, et al. "Protein Synthesis and Accumulation in Bean Cotyledons during Growth." Plant physiology vol. 61,6 (1978): 918-23. doi: https://doi.org/10.1104/pp.61.6.918
Sun SM, Mutschler MA, Bliss FA, Hall TC. Protein Synthesis and Accumulation in Bean Cotyledons during Growth. Plant Physiol. 1978 Jun;61(6):918-23. doi: 10.1104/pp.61.6.918. PMID: 16660426; PMCID: PMC1092012.
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Plant Physiol. 1978 Jun;61(6):918-23. doi: 10.1104/pp.61.6.918.

Protein Synthesis and Accumulation in Bean Cotyledons during Growth.

Plant physiology

S M Sun, M A Mutschler, F A Bliss, T C Hall

Affiliations

  1. Department of Horticulture, University of Wisconsin, Madison, Wisconsin 53706.

PMID: 16660426 PMCID: PMC1092012 DOI: 10.1104/pp.61.6.918

Abstract

Analysis of total protein, of specific proteins by gel electrophoresis and immunoelectrophoresis, and of protein synthetic activity in vitro confirmed that intense protein synthesis and accumulation occurred as the French bean (Phaseolus vulgaris L). seed grew from 12 to 20 millimeters. These techniques showed that there was no globulin-1 (G1) fraction (requiring high salt for solubility) present in 6-millimeter seeds, and only very small amounts were synthesized in seeds less than 9 millimeters long. The 7- to 9-millimeter stages represent a 2-day transition period over which genetic information for the G1 protein becomes actively expressed, accounting for at least 50% of all protein synthesized in this tissue during the following 14 days. At maturity, the electrophoretic analysis confirmed that G1 globulin was the major storage protein, representing some 50% of the dry seed protein. Cell-free protein synthesis assays, including immunoprecipitation of the in vitro products, clearly showed G1 polypeptides to be among the polysome-directed products.

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