Rhamnose binding protein

Details Rhamnose binding protein Rhamnose binding protein

2005-03-03

2008-03-25

Navarro, Mark (Department: 1645)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving antigen-antibody binding, specific binding protein...

C435S007230

Reexamination Certificate

active

07348152

ABSTRACT:
An isolated RBP with at least one of the following characteristics:a) a molecular weight of approximately 65-70 kDa and more preferably 66-69 kDa;b) a pI of greater than 10 or less than 3;c) a dissociation constant of approximately 1.5×10−6when bound to the rhamnose moiety of solamargine;d) adapted to bind to a rhamnose affinity column prepared according to example 1 and under the conditions set out therein;e) adapted to be eluted from the column in example 1 with a 100 mM rhamnose solution;f) insoluble in aqueous solution; andg) soluble in highly denaturing buffers containing greater that approximately 2% surfactant.

REFERENCES:
patent: 4861581 (1989-08-01), Epstein et al.
patent: 5225542 (1993-07-01), Cramer et al.
Kolb-Bachofen et al. “GalNAc/Gal-specific rat liver lectins: their role in cellular recognition”.Biology Cell, vol. 51, pp. 219-226 (1984).
Lehrman et al. “The binding of fucose-containing glycoproteins by hepatic lectins”.The Journal of Biological Chemistry, vol. 261, No. 16, pp. 7412-7418 (Jun. 1986).
Ashwell et al. “Carbohydrate-specific receptors of the liver”.Ann. Rev. Biochem, vol. 51, pp. 531-554 (1982).
Grillon et al., “Soluble human lymphocyte sugar binding proteins with immunosuppressive activity”.Immunology Letters, vol. 28, No. 1, pp. 47-56 (1991).
Weebadda et al. “Avian sac and plasma proteins that bind surface polysaccharides ofEscherichia coliO2”.Comparative Biochemistry and Physiology, Part B, vol. 130, pp. 299-312 (2001).
Komori et al. “Primary structure and biological active of snake venom lectin (APL) fromAgkistrodon p. piscivorus(eastern cottonmouth)”.Toxicon, vol. 37, pp. 1053-1064 (1999).
Amini et al. “Cryptic domains of a 60kDa heat shock protein ofHelicobacter pyloribound to bovine lactoferrin”.FEMS Immunology and Medical Microbiology, vol. 16, pp. 247-255 (1996).
Nitta et al. “Comparative studies of carbohydrate-binding proteins fromXenopus laevisskin and eggs. Sugar-binding specificities and affinity purification”.Chemical and Pharmaceutical Bulletin, vol. 38, No. 4, pp. 975-981 (1990).
Tobin et al. “Purification and properties of RhaR, the positive regulator of the L-Rhamnose operons ofEscherichia coli”. Journal of Molecular Biology, vol. 211, pp. 75-89 (1990).
Daikohara et al. “Comparative studies of the agglutination of tumor cells and erythrocytes byPlecoglossus altivelis(Ayu fish) roe lectin”.Physio-chemical Biology, vol. 37, No. 1, pp. 31-40 (1993).
Tateno et al.Journal of Biological Chemistry, vol. 273, No. 30, pp. 19190-19197 (Jul. 24, 1998).
Cham et al., Cancer Letters, 55:221-225 (1990).
Cham et al., Cancer Letters, 59:183-192 (1991).
Lin et al., Int. J. Peptide Protein Res., 12:311-317 (1978).
Nicolson et al., Biochemistry, 13(1):196-204 (1974).

Affiliated with

Also associated with

Rating

Rhamnose binding protein does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Rhamnose binding protein, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Rhamnose binding protein will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3961138