Biomedical subjects

J F Cavins

Publications and source records attributed to J F Cavins.

9 recordsLinked to original sources

PubMed1988

Nitrogen-to-protein conversion factors in animal feed and fecal samples.

Nitrogen-to-protein conversion factors were calculated for diets and fecal samples from three animal species fed low- or high-fiber diets. The conversion factors based on protein contents determined by amino acid analyses were calculated from total N (Kjeldahl analyses) and recovered amino acid plus NH3-N (amino acid analyses). Conversion factors based on protein contents determined by a fluorescamine assay for amino acids were also calculated from total Kjeldahl-N. The conversion factors based on Kjeldahl-N averaged 5.3 +/- .7 for the diets and 4.0 +/- .5 for the feces in the six animal and diet comparisons when calculated from anhydrous amino acid formula weights. The greatest deviations from the traditional 6.25 conversion factor occurred in the fecal samples of ruminant animals fed a corn-alfalfa meal diet at a maintenance level of intake. In contrast, conversion factors based on amino acid plus NH3-N were quite stable. These factors averaged 5.7 +/- .1 for feeds and 5.5 +/- .1 for feces when calculated from anhydrous amino acid residue weights.

Amino Acids↗

PubMed1986

Isolation and characterization of a soybean lectin having 4-O-methylglucuronic acid specificity.

A new lectin from soybeans having specificity toward the extracellular 4-O-methyl-D-glucurono-L-rhamnans produced by certain strains of Rhizobium japonicum has been purified and characterized. Isolation was accomplished initially by isoelectric precipitation of contaminating globulins and subsequently by affinity chromatography on partially hydrolyzed glucuronorhamnan covalently coupled to amino-hexylagarose. Residual globulins were removed by adsorption of the lectin on concanavalin A-agarose and elution with methyl alpha-mannoside. The lectin is a glycoprotein (3-5% carbohydrate) with a molecular weight of approximately 175 000. It is a tetramer with subunit molecular weights of 45 000 when dissociated with sodium dodecyl sulfate. Reverse-phase high-pressure liquid chromatography analysis indicates the presence of two types of subunits, both having equivalent molecular weights. According to amino acid analyses, the lectin is rich in acidic but low in sulfur-containing amino acids. The carbohydrate portion of the lectin contains mannose; no hexosamines could be detected. Chemical modification of the lectin indicated that neither sulfhydryl groups nor amino groups participate in binding. Quantitative binding studies of the lectin with various carbohydrate haptens showed that specificity was directed toward 4-O-methyl-D-glucuronic acid, D-glucuronic acid, and their methyl glycosides with 4-O-methyl-D-glucuronic acid 3-4-fold more effective. In each instance, the methyl glycoside is a more effective hapten.

Amino Acids↗

PubMed1976

Altered nitrogenous pools induced by the azolla-anabaena azolla symbiosis.

The free amino acid and ammonia pools of Azolla caroliniana were analyzed by quantitative column chromatography on columns capable of separating all of the nitrogenous constituents normally found in physiological fluids. Comparisons were made of plants containing symbiotic algae and grown on nitrogen-free media, plants grown on media containing nitrate, and algae-free plants also grown on nitrate media. The major feature of the data was a very high level of intracellular ammonia found in plants which contain N(2)-fixing algal symbionts. In addition to the more usual amino acids, serine and cystathionine were found in the free amino acid pool.

Journal Article↗

PubMed1971