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Biomedical subjects

C San José

Publications and source records attributed to C San José.

6 recordsLinked to original sources
PubMed1996

The mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans.

The Candida albicans HOG1 gene (HOG1CA) was cloned by functional complementation of the osmosensitive phenotype associated with Saccharomyces cerevisiae hog1 delta mutants. HOG1CA codes for a 377-amino-acid protein, 78% identical to S. cerevisiae Hog1p. A C. albicans hog1 null mutant was found to be sensitive to osmotic stress and failed to accumulate glycerol on high-osmolarity media.

Adaptation, Physiological↗
PubMed1988

Characterization of a pyoverdine-deficient mutant of Pseudomonas fluorescens impaired in the secretion of extracellular lipase.

A mutant of Pseudomonas fluorescens strain B52 deficient in the synthesis of the fluorescent pigment, pyoverdine, was isolated. Absence of pyoverdine and other siderophores was confirmed by gel filtration, a specific siderophore assay, and inhibition studies with the iron chelator EDDA. Both parent and mutant synthesized additional outer membrane proteins in response to iron-limitation. Mutant cells cultured in the absence of iron(III) accumulated 55Fe-labeled pyoverdine. The mutant produced extracellular proteinase normally on various media, but was deficient in lipase secretion. Growth of the mutant with partially-purified pyoverdine resulted in a 2.5-fold stimulation of lipase secretion. The mutant grew poorly in deferrated medium; however, the addition of iron(III) stimulated growth. Proteinase secretion in deferrated medium was stimulated over a narrow range of iron(III) concentration, while lipase secretion was only slightly affected. The data suggest that separate regulatory mechanisms exist for the control of proteinase and lipase secretion by iron(III).

Cell Membrane↗
PubMed1978

Storage of lactose-hydrolysed dried milk: effect of water activity on the protein nutritional value.

The retention of the protein nutritional value during storage of lactose-hydrolysed dried milk at different water activities (aw) was studied and compared with that of ordinary milk. In the lactose-hydrolysed milk biologically available lysine decreased much more rapidly than in the ordinary milk at all the different aw studied. Thus, at conditions normally accepted for ordinary dried milk (aw approximately 0.2; moisture approximately 4%) there was an available lysine loss in the hydrolysed milk of about 25% after 2 months and about 40% after 6-months storage at room temperature. This occurred without any visible browning. It is concluded that drying to very low aw (less than or equal to 0.11) is necessary to obtain good stability of the protein nutritional value (PNV) in lactose-hydrolysed milk. The drying, however, must be done so that losses in nutritional value are minimal during that process. It should also be noted that fat oxidation might be a problem at such low aw. A chemical method for available lysine assay (guanidination and assay of homoarginine) gave values in good agreement with the biological evaluations with rats.

Animals↗