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|Title:||Storage Proteins in Apple Trees (Woody Plant, Nitrogen, Senescence)|
|Department / Program:||Horticulture|
|Degree Granting Institution:||University of Illinois at Urbana-Champaign|
|Subject(s):||Biology, Plant Physiology|
|Abstract:||This study was undertaken to elucidate into the mode of accumulation and subsequent degradation of storage proteins in apple trees. Protein isolation, characterization, and proteolytic enzyme study were involved.
The prominent proteins present in shoot bark were the MWs 56, 38, 28, and 20 kD. These 4 proteins constituted a high proportion of the total protein in bark increasing from 46 to 70% of the total protein during senescence. The 4 major proteins appeared to serve a storage role and consisted of many heterogeneous polypeptides of different isoelectric points. Twenty one, thirteen, seven, and twenty one heterogeneous polypeptides were found in those 4 major proteins, respectively. Each of the 4 major proteins had similar amino acid composition in their hydrolysates with approximately 40% of the total protein in basic amino acids, asparagine, glutamine, and their amides. The highest proteolytic activity was found when the 20 kD protein were used as a substrate.
During regrowth, a slightly greater degradation of the four dominant proteins was observed. A preferential degradation of some bark proteins differing in electrical charges was also found. Nonetheless, the protein degradation was not limited to a few protein species.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1985.
|Date Available in IDEALS:||2014-12-16|