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Transparent gels containing about 2% protein were obtained by mixing alkaline dope solution of 7S or 11S soybean proteins with alcohol. The 7S component showed the ability to form a stronger gel than the 11S. This phenomenon depended on pH and alcohol concentration. In 66 % ethanol, the viscosity of the 7S and 11S reached maxima at pH 11.4 and 11.2, respectively. Above these pH levels where further unfolding and dissociation into subunits of the protein molecules occur, the viscosity decreased rather. The effectiveness of alcohol to increase viscosity increased in the order; n-butanol < tert-butanol < n-propanol < iso-propanol < ethanol < methanol. Alcohols having minor hydrophobicity were more effective for increasing viscosity, but ethylene glycol was ineffective. The addition of NaCl or 2-mercaptoethanol to ethanol-mixed alkaline dope solutions resulted in the remarkable increment of the viscosity, especially for the 7S.  相似文献   
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Primary culture of rat hepatocyte was performed in an oxygen-permeable film dish (F-dish), which would be expected to give an oxygen-rich culture condition. In the conventional culture dish in which the depth of medium was 2 mm, the oxygen tension (pO2) in the medium decreased from 19% (144 mmHg) to 0.3% (2.3 mmHg) within 2 hr, while the pO2 in the F-dish maintained 8.5% (64.6 mmHg) even after 2 hr. The adverse effect of the oxygen-deficiency appeared in the albumin secretion activity of the hepatocytes and it was more remarkable in the early period of culture. The average rate of albumin secretion for the initial 48 hr was 2.0 μg ml-1 hr-1 or 96 μg 106 cells-1 day-1 in the F-dish. The average rate of albumin secretion for the initial 12 hr was only 0.36 μg ml-1 hr-1 in the conventional culture dish. The activity of ammonia elimination in the F-dish was 20–50% higher than the conventional culture dish. Three-dimensional aggregate was formed only in the F-dish. The advantage of three-dimensional aggregate for albumin secretion was not clear compared with two-dimensional monolayer. This revised version was published online in July 2006 with corrections to the Cover Date.  相似文献   
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To characterize aspartyl aminopeptidase from Aspergillus oryzae, the recombinant enzyme was expressed in Escherichia coli. The enzyme cleaves N-terminal acidic amino acids. About 30% activity was retained in 20% NaCl. Digestion of defatted soybean by the enzyme resulted in an increase in the glutamic acid content, suggesting that the enzyme is potentially responsible for the release of glutamic acid in soy sauce mash.  相似文献   
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Abstract

A partially self-complementally decadeoxyribonucleotide, d(pCGACCCGGGT) has been 3′-blocked with the acetyl group and joined to d(CGACCCGGGT) to yield an eicosadeoxyribonucleotide duplex which contained recognition sites for six restriction enzymes.  相似文献   
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