pH-dependent molecular weight changes of κ-casein glyco-macropeptide and its preparation by ultrafiltration
Yuki KawasakiHiroyuki KawakamiMorimasa TanimotoShun’ichi DosakoAkira TomizawaMunio KotakeIwao Nakajima
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Biological activity of bovine κ-caseino glycomacropeptide (GMP) has received much attention in recent years. Research has focused on the ability of GMP to bind cholera and Escherichia coli enterotoxins, inhibit bacterial and viral adhesion, suppress gastric secretions, promote bifidobacterial growth and modulate immune system responses. Of these, protection against toxins, bacteria, and viruses and modulation of the immune system are the most promising applications.
Cholera toxin
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Journal Article Inhibition by κ-Casein Glycomacropeptide and Lactoferrin of Influenza Virus Hemagglutination Get access Yoshihiro Kawasaki, Yoshihiro Kawasaki Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, Japan Search for other works by this author on: Oxford Academic Google Scholar Hiroko Isoda, Hiroko Isoda Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, JapanSapporo Research Laboratory, Snow Brand Milk Products Co., Ltd., 6–1–1 Naebo, Higashi-ku, Sapporo 065, Japan Search for other works by this author on: Oxford Academic Google Scholar Hiroshi Shinmoto, Hiroshi Shinmoto Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, Japan Search for other works by this author on: Oxford Academic Google Scholar Morimasa Tanimoto, Morimasa Tanimoto Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, Japan Search for other works by this author on: Oxford Academic Google Scholar Shun'ichi Dosako, Shun'ichi Dosako Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, Japan Search for other works by this author on: Oxford Academic Google Scholar Tadashi Idota, Tadashi Idota Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, Japan Search for other works by this author on: Oxford Academic Google Scholar Ichiro Nakajima Ichiro Nakajima Technical Research Institute, Snow Brand Milk Products Co., Ltd., 1–1–2 Minamidai, Kawagoe 350–11, Japan Search for other works by this author on: Oxford Academic Google Scholar Bioscience, Biotechnology, and Biochemistry, Volume 57, Issue 7, 1 January 1993, Pages 1214–1215, https://doi.org/10.1271/bbb.57.1214 Published: 01 January 1993 Article history Published: 01 January 1993 Received: 07 January 1993
Lactoferrin
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ABSTRACT Glycomacropeptide (GMP) was isolated from crystalline rennin and microbial rennet hydrolyzed caseinate and skim milk by Sephadex gel filtration, DEAE Sephadex ion exchange chromatography, Con A‐Sepharose affinity chromatography and exhaustive dialysis and characterized by size exclusion and reversed phase high performance liquid chromatography (HPLC) and sodium dodecyl sulfate gel electrophoresis (SDS PAGE). Size exclusion HPLC revealed one major GMP peak with a molecular weight of 33,000 daltons. SDS PAGE revealed a group of size‐heterogeneous peptides with molecular weights of < 18,000 daltons. Reversed phase HPLC revealed one major GMP peak with several minor peptides, indicating heterogeneity with respect to hydrophobicity/polarity.
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Sodium dodecyl sulfate
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Various caseinoglycopeptide derivatives prepared from mammalian milk were evaluated as inhibitors of hemagglutinations mediated by Actinomyces viscosus Ny1, Streptococcus sanguis OMZ9, and, for comparative purposes, plant lectins from Arachis hypogaea and Bauhinia purpurea. It was found that recognition of the beta-D-galactose-(1----3)-2-acetamido-2-deoxy-D-galactose carbohydrate chain by Actinomyces viscosus Ny1 organisms and Arachis hypogaea and B. purpurea agglutinins had similar structural requirements; in all cases, the desialylated bovine caseinoglycomacropeptide, on which several units of the above mentioned disaccharide are clustered, behaved as the most potent hemagglutination inhibitor. By contrast, none of the preparations tested inhibited erythrocyte agglutination by S. sanguis OMZ9. Thus, the desialylated bovine caseinoglycomacropeptide acts as a potent and specific inhibitor of oral Actinomyces adhesion to cell membranes (a soft surface) and could be used as a probe for the study of recognition mechanisms mediated by Actinomyces galactose-binding lectins. During the present study, both native and desialylated variants of the same bovine glycomacropeptide also totally prevented the adhesion of Actinomyces viscosus Ny1, S. sanguis OMZ9, and S. mutans OMZ176 to polystyrene surfaces. Comparative evaluations of various structurally different compounds gave the following results. Neither mono- nor disaccharides related to caseinoglycopeptide carbohydrates prevented adhesion; highly positively or negatively charged polypeptides and polysaccharides were either not or only moderately active. Besides these glycomacropeptides, an inhibitory activity was also exhibited by other mucin-type glycoproteins carrying short O-linked carbohydrate chains (including bovine submaxillary mucin), polyethylene glycol, and bovine serum albumin. Consequently, caseinoglycopeptide prevention of oral bacterial adhesion to polystyrene tubes (a hard surface) takes place with no species specificity and can be compared to nonspecific inhibition exhibited by various polymers with very different structural characteristics.
Bovine serum albumin
Actinomycetaceae
Agglutination (biology)
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Rennet
Functional food
Health Benefits
Proteolysis
Food protein
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Ion chromatography
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Diafiltration
Tissue transglutaminase
Ultrafiltration (renal)
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Inhibition from binding of Cholera toxin (CT) to Chinese hamster ovary (CHO)-K1 cells and ganglioside GM1 by lactoferrin (Lf) and kappa-casein glycomacropeptide (GMP) from cow's milk was examined. Both Lf and GMP effectively reduced the CT-derived morphological changes in CHO-K1 cells. The competitive binding assay demonstrated that both Lf and GMP inhibited the binding of CT to GM1, although their affinity for CT was lower than that of GM1. The inhibitory effect of Lf and GMP seemed to be attributed to their terminal sialic acid, although the sugar chain sequence only partially fitted to the CT-receptor.
Cholera toxin
Ganglioside
Lactoferrin
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