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R Jenness

Publications and source records attributed to R Jenness.

At least 37 records · Page 2Linked to original sources

Comparative aspects of milk proteins.

The current status of knowledge of the major proteins of milks of various species is evaluated. Most of the non-bovine milk proteins are homologous with the recognized families of those of Bos taurus, alpha S1-caseins, alpha S2-caseins, beta-caseins, kappa-caseins, beta-lactoglobulins, and alpha-lactalbumins, each family representing a separate genetic locus specific to the mammary gland. No prominent milk protein not homologous to one of these families has yet been discovered in milk of any species. Genetic polymorphism resulting from substitutions in the polypeptide chains and various degrees of post-translational phosphorylation, glycosylation, and proteolysis have been identified in milk proteins of several species. Total protein production ranges among species from about 0.5 to 10 g/d per kg0.75 maternal weight. Proportions of the several proteins vary greatly among species, but few accurate analytical data are available except for total casein and total whey protein contents.

Amino Acids↗

The composition of human milk.

Mature human milk contains 3%--5% fat, 0.8%--0.9% protein, 6.9%--7.2% carbohydrate calculated as lactose, and 0.2% mineral constituents expressed as ash. Its energy content is 60--75 kcal/100 ml. Protein content is markedly higher and carbohydrate content lower in colostrum than in mature milk. Fat content does not vary consistently during lactation but exhibits large diurnal variations and increases during the course of each nursing. Race, age, parity, or diet do not greatly affect milk composition and there is no consistent compositional difference between milks from the two breasts unless one is infected. The principal proteins of human milk are a casein homologous to bovine beta-casein, alpha-lactalbumin, lactoferrin, immunoglobulin IgA, lysozyme, and serum albumin. Many enzymes and several "minor" proteins also occur. The essential amino acid pattern of human milk closely resembles that found to be optimal for human infants. Possible special functions of milk proteins and enzymes other than as a source of amino acids, are as yet largely speculative. The principal sugar of human milk is lactose but 30 or more oligosaccharides, all containing terminal Gal-(beta 1,4)-Glc and ranging from 3--14 saccharide units per molecule are also present. These may amount in the aggregate to as much as 1 g/100 ml in mature milk and 2.5 g/100 ml in colostrum. Some of them may function to control intestinal flora because of their ability to promote growth of certain strains of lactobacilli. Human milk fat is characterized by high contents of palmitic and oleic acids. the former heavily concentrated in the 2-position and the latter in the 1- and 3-positions of the triglycerides. Fatty acid composition of milk fat varies somewhat with the composition of diet, particularly the fatty acids which it supplies. Phospholipids, amounting in the aggregate to about 75 mg/100 ml, include phosphatidyl ethanolamine, phosphatidyl choline, phosphatidyl serine, phosphatidyl inositol, and sphingomyelin. The principal mineral constituents of human milk are Na, K, Ca, Mg, P, and Cl. Calcium concentrations reported in various studies vary from 25--35 mg/100 ml. Phosphorus at 13--16 mg/100 ml is much more constant but is lower in proportion to casein and calcium than in milks of most other species. Iron, copper, and zinc contents of human milk vary considerably. A long list of other trace elements has been reported. About 25% of the total nitrogen of human milk represents nonprotein compounds including urea, uric acid, creatine, creatinine, and a large number of amino acids. Of the latter, glutamic acid and taurine are prominent. All of the vitamins, except K, are found in human milk in nutritionally significant concentrations.

Animals↗

Ascorbic acid and L-gulonolactone oxidase in lagomorphs.

1. The activity of L-gulonolactone oxidase (EC 1.1.3.8) in the liver of eastern cottontail rabbits (Sylvilagus floridanus) is about 10-fold greater in winter than in summer. 2. L-gulonolactone oxidase activity is low and tissue ascorbate high during all seasons in snowshoe hares (Lepus americanus). 3. Liver contents of ascorbate fall to low levels in L. americanus fed on rabbit chow in the laboratory. 4. The activity of L-gulonolactone oxidase in liver of Sylvilagus and Oryctolagus is depressed by feeding high levels of L-ascorbic acid. 5. The New Zealand White breed of domestic rabbit (Oryctolagus cuniculus) has considerably higher levels of L-gulonolactone oxidase and liver ascorbate than does the Dutch breed. 6. In a wild population of Oryctolagus sampled in Australia L-gulonolactone oxidase levels were intermediate between those of the two domestic breeds and more variable than either.

Animals↗

Isolation of kappa-casein-like proteins from milks of various species.

Kappa-Casein-like proteins were isolated from the milks of cow, goat, reindeer, horse, rat, and rabbit. When treated with rennin, all of the isolated kappa-casein components yielded para-kappa-casein-like bands on gel electrophoresis. The rate of cleavage of these components with rennin was determined by measuring material soluble in trichloroacetic acid (macropeptide). The curves were characteristic of a limited, specific attack by rennin on these proteins. The goat and reindeer kappa-caseins were nearly as bovine kappa-casein, but the cleavage of horse, rat, and rabbit kappa-casein-like components was much slower.

Animals↗

Rennin and pepsin in stomachs of rats (Rattus norvegicus).

The predominant protease in adult rat stomachs has a pH optimum of 2.0 to 2.3 which corresponds almost exactly to that of porcine pepsin. One-day-old rats have a protease with a pH optimum of 3.8 to 4.2 similar to that of calf rennin. The pH optimum of rat stomach proteases decreases with age, and at 28 days it is similar to that of the adult. The pH of stomach contents of rats decreases with age from pH 5.8 to pH 4.6. These data support the contention by other workers that the onset of pepsin secretion is a prerequisite for weaning and that rennin-like enzymes are not unique to ruminant species.

Age Factors↗

Isolation, composition and functional properties of alpha-lactalbumins from several species.

1. Galactosyltranferases were isolated from bovine and pig milk and alpha-labtalbumins from milks of cow, pig, dog, rabbit, baboon and chimpanzee. 2. Alpha-Lactalbumins were characterized by gel electrophoresis, amino acid composition, ultraviolet absorbance, and ability to promote synthesis of lactose by the galactosyltransferases. 3. The order of K-m values of the various alpha-lactalbumins was the same with both cow and pig galactosyltransferases and differed from the order predicted from taxonomical classification of the species. 4. A280/A260 abosrbance ratios were correlated with K-m values suggesting involvement of tyrosyl groups in the function of alpha-lactalbumin.

Amino Acids↗