1987 Fiscal Year Final Research Report Summary
Comparative Biochemistry and Nutritional Properties of Milk Proteins
| Project/Area Number |
60480083
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
畜産化学
|
|---|
| Research Institution | University of Tokyo |
|---|
Principal Investigator |
YAMAUCHI Kunio University of Tokyo, Professor, 農学部, 教授 (60011821)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
SHIMIZU Makoto University of Tokyo, Research Associate, 農学部, 助手 (30114507)
KAMINOGAWA Shuichi University of Tokyo, Associate Professor, 農学部, 助教授 (50011945)
AZUMA Norihiro University of Tokyo Research Associate, 農学部, 助手 (30151062)
|
|---|
| Project Period (FY) |
1985 – 1987
|
| Keywords | Milk proteins / Comparative biochemistry / Human nilk / <beta>-Casein / <kappa>-Casein / <alpha>-Lactalbumin / Monoclonal antibody / 乳脂肪球膜蛋白質 |
|---|
| Research Abstract |
1. Positive correlation between the phosphate content and calcium binding capacity of human <beta>-casein was observed. The precipitability in the presence of Ca also correlated with the phosphate content. The Ca-induced precipitation of <beta>-casein of higher phosphate content was prevented by that of lower phosphate content. No significant difference in the digestibility of <beta>-casein was observed among the molecules having different phosphate content. Bovine <beta>-casein showed similar digestibility to human <beta>-casein. Monoclonal antibodies prepared to bovine <beta>-casein did not recognize human <beta>-casein.
2. Heterogeneity of the carbohydrate chains in human <kappa>-casein was observed by haemagglutination- inhikbition test using lectins and thermolysin-digested blycopeptides of <kappa>-casein. Reconstituted micelles formed by <kappa>- and <beta>-caseins were bigger when the <beta>/<kappa> ratio was higher. Smaller micelles contained <kappa>-casein of less carbohydrate
… More
content.
3 A monoclonal antibody was prepared against bovine <alpha>-lactalbumin, and its reactivity with <alpha>-lactalbumin from different animal milks was determined. Binding activity of <alpha>-lactalbumin from different species with the monoclonal antibody was in the order of bovine>goat>giraffe>horse>monkey>human> guines pig. Evolutional distances between bovine <alpha>-lactalbumin and other <alpha>-lactalbumins estimated from their amino acid composition were in agreement to the results obtained by using the monoclonal antibody.
4. Human milk serum and fat globule membrane were observed to contain two high-emolecular weight mucin-like blycoproteins, HMGP-A and C. Reactivity with several monoclonal antibodies and susceptibility to various proteolytic enzymes were different between the two HMGP, although the profiles of their chemical composition resembled to each other. HMGP was not detected in bovine milk. The reversed-phase high performance liquid chromatography was useful for purification and detection of HMGP. HMGP-A and C showed a growth inhibitory activity to mouce 3T3 cells. Less
|
