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Biomedical subjects

M L Groves

Publications and source records attributed to M L Groves.

14 recordsLinked to original sources
PubMed1992

Reexamination of the polymeric distributions of kappa-casein isolated from bovine milk.

kappa-Casein the stabilizing protein of the colloidal milk protein complex was purified from bovine skim milk by the method of McKenzie and Wake (Biochim, Biophys. Acta. 47, 240, 1961). The preparations were examined by sodium dodecyl sulfate gel electrophoresis in the presence and absence of a reducing agent. In the presence of a reducing agent, the kappa-casein migrates as a single low molecular weight band. However, in the absence of a reducing agent, a characteristic pattern of aggregates of varying molecular weight was observed with components ranging from monomer to octamer in integer steps. Densitometry of the Coomassie blue stained gels showed an almost equal distribution of components in each band; carbohydrate staining showed preferential location of sugar residues in lower molecular weight components. Treatment with chymosin (rennin) caused a downward shift in apparent molecular weight for each band with no change in the relative intensity of the Coomassie blue stained bands. Similar gel patterns were observed in whole caseins and partially purified kappa-caseins, indicating that this size distribution is a natural disulfide-linked reporter for the distribution of kappa-casein in casein colloids (micelles).

Animals↗
PubMed1988

The calcium-dependent electrophoretic shift of alpha-lactalbumin, the modifier protein of galactosyl transferase.

alpha-Lactalbumin, the modifier protein of galactosyl transferase in the synthesis of lactose by the mammary gland, has been shown to undergo a Ca2+-dependent electrophoretic shift. Such shifts, characteristic of most calcium modulated proteins, are related to gross conformational changes upon binding calcium when detected in the presence of detergent (SDS-PAGE). However, we detected the calcium shift for alpha-lactalbumin using non-denaturing PAGE (ND-PAGE) where electrical charge changes are observed upon binding calcium. In order for a shift to be observed between the apo and calcium bound protein, calcium ion binding to proteins must have minimal dissociation constants (Kdiss) of 10(-7) M; alpha-lactalbumin is reported to bind calcium at Kdiss = 10(-10) to 10(-12) M. The electrophoretic shift identifies alpha-lactalbumin in complex milk whey patterns of many species of mammals.

Animals↗
PubMed1985

Effect of temperature on the circular dichroism spectra of beta 2-microglobulins.

When the temperature was lowered from 25 to 5 degrees C dramatic changes were observed in the near-ultraviolet circular dichroism spectra of bovine and caprine but not human beta 2-microglobulin. Comparison of the protein sequences suggests that the conformational change occurs in the amino-terminal 24 residues and that a tyrosine residue located on a potential beta-turn acts as a reporter group. Because delta H degrees is small (-22 kcal X mol-1), such conformational changes, possibly not readily observed, may occur at low temperatures in other proteins having potential beta-turns in otherwise aperiodic regions of sequence.

Animals↗
PubMed1985

Isolation and characterization of new proteins produced by the infusion of colchicine in goat mammary gland.

Three new proteins have now been isolated from goat milk obtained after colchicine is infused into the mammary gland. Two of the proteins are proline-rich, and a third is a very acidic phosphoprotein. One of the proline-rich proteins is related compositionally to a sheep colostrum proline-rich protein, which has been shown to have a regulatory effect on the immune response (Janusz, M., Stavoscik, K., Zimecki, M., Wieczorek, Z., and Lisowski, J. (1981) Biochem. J. 199, 9-15). Other aspects of colchicine-treated milks are described.

Amino Acids↗
PubMed1985

Isolation and properties of goat beta 2-microglobulin.

Goat beta 2-microglobulin was isolated and purified from colostrum. Comparisons of the amino acid composition and amino-terminal sequence of the goat protein with the bovine and human homologues, indicates a high degree of similarity. Both goat and bovine beta 2-microglobulins differ slightly in composition from the human molecule, most notably in threonine and proline values. For the first 32 residues, bovine and goat differ only at two positions, one of which is a valyl/isoleucyl substitution consistent with the amino acid compositions. The equivalent goat/human sequence comparison shows seven differences. Immunological studies, using the ELISA method, also confirm the close relatedness of goat and bovine beta 2-microglobulin and their more distant relatedness to the human homologue.

Amino Acid Sequence↗
PubMed1979

Human beta-casein.

Human beta-casein occurs in multiphosphorylated forms having the same amino acid composition but with 0-5 phosphate groups/molecule. Sequence analysis was used to determine whether each of the phosphorylated forms is a mixture of species having a certain number of phosphate groups randomly distributed or whether each form contains phosphate groups on specific seryl or threonyl residues. It was found that forms containing 2, 4 and 5 phosphate groups/molecule are homogeneous with respect to their phosphorylation sites. The monophosphorylated form, however, is a mixture of equal amounts of species phosphorylated at residues 9 or 10.

Amino Acid Sequence↗
PubMed1978

Isolation, composition and ordering of cyanogen bromide peptides in human casein.

The major component of the casein fraction of human milk was cleaved by cyanogen bromide, and the composition of the resulting peptides was determined. Casein was also subjected to limited digestion by trypsin, and the amino acid composition of the isolated peptides was established. With this information the peptides were ordered as they occur in the purified protein.

Amino Acids↗
PubMed1977

Studies on human alpha-lactalbumin: radioimmunoassay measurements in normal human breast and breast cancer.

A sensitive and specific radioimmunoassay for human alpha-lactalbumin, a milk protein, has been developed in order to examine the effect of prolactin on the human breast in normal and diseased states. Samples of milk from nursing mothers and from men and women with galactorrhea were found to contain milligram concentrations of this protein. In serum, 8 of 25 normal men and 18 of 44 normal women had detectable concentrations of alpha-lactalbumin. Significantly higher levels of alpha-lactalbumin were found in 17 of 19 women during pregnancy who were not actively lactating. All nursing mothers were found to have distinctly elevated serum alpha-lactalbumin concentrations. In a group of 17 female patients with phenothiazine induced prolactin elevations (mean 29.4 ng/ml), the mean serum alpha-lactalbumin of 17.3 ng/ml was significantly higher than in normal female volunteers. Patients with gynecomastia were not noted to have elevated alpha-lactalbumin. In vitro, homogenates of normal breast and carcinoma tissue from the same individuals revealed that in 9 of 17 patients alpha-lactalbumin was present in higher concentrations in normal than in cancerous tissue. Overall, alpha-lactalbumin was found in 48.5% of homogenates and 41% of organ cultures of normal breast tissue from cancer patients. In contrast, it was present in only 19% of homogenates and 21% of cultures of carcinoma tissue, indicating that the cancer tissue may lose its ability to produce alpha-lactalbumin. Differences in biologic behavior were found in some tumors. In 2 cases homogenates of breast cancer tissue had much higher concentrations of alpha-lactalbumin than the normal tissue, and in 3 of 33 tumors studied in organ culture prolactin increased alpha-lactalbumin output.

Adolescent↗
PubMed1976

Amino terminal sequence and location of phosphate groups of the major human casein.

The amino acid sequence of the first 28 residues of the major human casein was determined. This protein in multiphosphorylated forms (0 to 5 phosphorous per molecule) was compared to cow beta-casein which is similar in composition but phosphorylated at a constant level. After sequencing the phosphate-free human casein, phosphorylated seryl and threonyl residues were located in three of the other phosphorylated forms by examining the aqueous layer of the phenylthiohydantoin conversion step during automatic liquid phase sequencing. Phosphate groups on specific seryl/threonyl residues suggest a biosynthetic mechanism involving stepwise phosphorylation or dephosphorylation.

Amino Acid Sequence↗