Role of Basic Residues of Human Lactoferrin in the Interaction with B Lymphocytes
スポンサーリンク
概要
- 論文の詳細を見る
We have previously demonstrated that lactoferrin was incorporated into B lymphocytes and that a trypsin treatment for a short period reduced the number of lactoferrin molecules incorporated into B lymphocytes. An N-terminal sequence analysis revealed that the mild trypsin treatment had cleaved the three N-terminal amino acids, Gly^1-Arg^2-Arg^3. Chemical conjugation of lost sequence analogue Gly-Arg-Arg-Gly with the mildly digested lactoferrin recovered the interaction with B lymphocytes, while conjugation of acetyl-Arg-Arg-Gly, a deamino analogue of Gly-Arg-Arg-Gly, did not recover the interaction. This shows that the N-terminal basic region containing N-terminal Gly played an important role in the interaction with B lymphocytes. Acylation of the amino groups of lactoferrin also significantly reduced the interaction with B lymphocytes, and an O-methylisourea treatment of the amino groups, which preserved the positive charge, hardly affected the interaction. These results suggest that both the N-terminal basic region and the basic characteristics of the whole molecule contributed to its interaction with B lymphocytes.
- 社団法人日本農芸化学会の論文
- 2000-02-23
著者
-
KAWASAKI Yoshihiro
Technology and Research Institute, Snow Brand Milk Products Co., Ltd.
-
SHINMOTO Hiroshi
Technical Research Institute, Snow Brand Milk Products Co., Ltd.
-
Kawasaki Yoshihiro
Technical Research Institute Snow Brand Milk Products Co. Ltd.
-
Kawasaki Yoshihiro
Technical Research Institute Snow Brand Milk Products Co.
-
Kawasaki Y
Snow Brand Milk Products Co. Ltd. Saitama Jpn
-
SATO Kaoru
Technical Research Institute, Snow Brand Milk Products Co., Ltd.
-
DOSAKO Shunichi
Technical Research Institute, Snow Brand Milk Products Co.
-
Dosako Shunichi
Technical Research Institute Snow Brand Milk Products Co.
-
Dosako Shunichi
Technical Research Institute Snow Brand Milk Products Co. Ltd.
-
Sato Kaoru
Technical Research Institute Snow Brand Milk Products Co. Ltd.
-
Shinmoto Hiroshi
Technical Research Institute Snow Brand Milk Products Co. Ltd.
関連論文
- Milk Calcium Taken with Cheese Increases Bone Mineral Density and Bone Strength in Growing Rats(Food & Nutrition Science)
- Generation of Human-mouse Hybridoma Secreting Human IgM Class Anti-neocarzinostain Anti-body and Its Application to Hybrid Hybridoma(Biological Chemistry)
- 60-GHz Virtual Common-Drain-Biased Oscillator Design Using an Empirical HEMT Model
- 60-GHz HEMT-Based MMIC One-Chip Receiver
- Characteristics of Lipase Modified with Water-soluble Acylating Reagents and Its Esterification Ability
- Production of Pentameric Hybrid Immunoglobulins Consisting of IgA and IgM(Biological Chemistry)
- Inhibition by K-Casein Glycomacropeptide and Lactoferrin of Influenza Virus Hemagglutination
- Anti-oxidant Activity of Bovine Lactoferrin on Iron/Ascorbate Induced Lipid Peroxidation
- Inhibition by Bovine Lactoferrin of Adhesion of L929 Cells Cultured in Serum-free GIT Medium
- Uptake and Re-secretion of Human Lactoferrin by B Lymphocytes(Biological Chemistry)
- Selection of Fusion Partner Cell Lines for Generation of Human-Human Hybridomas that Secrete IgA(Biological Chemistry)
- Human-Human Hybridomas Secreting IgM-like Immunoglobulin with α and μ Heavy Chains(Biological Chemistry)
- Enzymatic Peptide Synthesis with Fatty Acid-modified Chymotrypsin and Trypsin in Aqueous-organic Media
- Enzymatic Functions of Fatty Acid-modified Chymotrypsin and Trypsin in Aqueous-organic Media
- Inhibition by Lactoferrin and κ-Casein Glycomacropeptide of Binding of Cholera Toxin to its Receptor
- Characteristics of Chymotrypsin Modified with Water-soluble Acylating Reagents and Its Peptide Synthesis Ability in Aqueous Organic Media
- Large-scale Preparation of κ-Casein Glycomacropeptide from Rennet Casein Whey
- Inhibitory Effects of Bovine Lactoferrin on the Adherence of Enterotoxigenic Escherichia coli to Host Cells
- Role of Basic Residues of Human Lactoferrin in the Interaction with B Lymphocytes
- Transformation of Human Colostrum Lymphocytes with Epstein-Barr Virus
- Effects of Ionic Strength on Thermostability of Lactoperoxidase