Analysis of the specificity of five murine anti-blood group A monoclonal antibodies, including one that identifies type 3 and type 4 A determinants

Biochemistry ◽  
1985 ◽  
Vol 24 (26) ◽  
pp. 7820-7826 ◽  
Author(s):  
Koichi Furukawa ◽  
Henrik Clausen ◽  
Senitiroh Hakomori ◽  
Junichi Sakamoto ◽  
Katherine Look ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Blood Group A ◽  
Group A ◽  
Type 3

scholarly journals Improved procedure for the construction of neoglycolipids having antigenic and lectin-binding activities, from reducing oligosaccharides

1988 ◽  
Vol 256 (2) ◽  
pp. 661-664 ◽  
Author(s):  
M S Stoll ◽  
T Mizuochi ◽  
R A Childs ◽  
T Feizi
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Concanavalin A ◽  
Lectin Binding ◽  
Blood Group A ◽  
Naturally Occurring ◽  
Group A ◽  
High Mannose ◽  
B Blood Group

Conditions have been established for the rapid and efficient conjugation of reducing oligosaccharides (di- to deca-saccharides) to dipalmitoyl phosphatidylethanolamine. The resulting neoglycolipids derived from several naturally occurring oligosaccharides and a series of N-linked high-mannose-type oligosaccharides released by hydrazinolysis from RNAase B showed specific and potent reactivities, as appropriate, with monoclonal antibodies to blood group Lewis(b), blood group A or a stage-specific embryonic (SSEA-1) antigen, or the lectin concanavalin A.

scholarly journals Some monoclonal antibody reagents (C219 and JSB-1) to P-glycoprotein contain antibodies to blood group A carbohydrate determinants: a problem of quality control for immunohistochemical analysis.

1991 ◽  
Vol 39 (12) ◽  
pp. 1603-1610 ◽  
Author(s):  
C L Finstad ◽  
B W Yin ◽  
C M Gordon ◽  
M G Federici ◽  
S Welt ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Blood Group ◽  
Immunohistochemical Analysis ◽  
Blood Type ◽  
Polymorphic Variation ◽  
Blood Group A ◽  
P Glycoprotein ◽  
Apparent Correlation ◽  
Group A ◽  
Type 3

Monoclonal antibodies (MAb) C219 and JSB-1 have been used extensively in the analysis of P-glycoprotein expression in normal and malignant tissues. This study demonstrates that some commercial lots of these MAb, even those supplied as purified immunoglobulins, contain contaminating anti-A blood group antibodies. In both sources of reagent, the antibody was specific for a particular A structure, known as repetitive or Type 3 A. These observations may account for earlier studies showing polymorphic variation in P-glycoprotein expression in epithelial tissues and an apparent correlation with the A blood type of the donor. Such reactivity can be eliminated by absorption of anti-P-glycoprotein reagents with A erythrocytes. These data re-emphasize the importance of evaluating MAb samples for unsuspected contaminating antibodies.

scholarly journals Human Cervical Epidermal Carcinoma-associated Intracellular Localization of Glycosphingolipid with Blood Group A Type 3 Chain

1993 ◽  
Vol 84 (6) ◽  
pp. 664-672 ◽  
Author(s):  
Yongxi Cui ◽  
Hiroshi Noguchi ◽  
Kazushige Kiguchi ◽  
Daisuke Aoki ◽  
Nobuyuki Susumu ◽  
...  
Keyword(s):  
Blood Group ◽  
Intracellular Localization ◽  
Blood Group A ◽  
Group A ◽  
Type 3 ◽  
Epidermal Carcinoma

Monoclonal Antibodies Against Blood Group A Secretors and Nonsecretors Saliva

2003 ◽  
Vol 22 (3) ◽  
pp. 183-186 ◽  
Author(s):  
Takeshi Ohmori ◽  
Hiroko Iwanari ◽  
Rie Aoi ◽  
Tomoko Shiraishi ◽  
Yukio Ito ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Blood Group A ◽  
Group A

Properties of Lectins from Snails of the Genus Helix Probed by Monoclonal Antibodies

1985 ◽  
Vol 40 (3-4) ◽  
pp. 254-261
Author(s):  
Hansjörg A. W. Schneider
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Double Diffusion ◽  
Cell Surfaces ◽  
Blood Group A ◽  
Antigenic Properties ◽  
Group A

Abstract Helix-Lectins, Monoclonal Antibodies against Lectins, C om petition between Antibodies and Carbohydrates Monoclonal antibodies were raised against the lectin of H elix pom atia (HPL). Besides anti­ bodies bearing the more common y and x chains, antibodies with a, /j. and X2 chains were elicited. The anti-HPL antibodies are expected to be useful in studies on HPL biogenesis and HPL sub­ structure and in studies concerned with the binding of HPL to cell surfaces. Binding of carbohydrates to HPL im paired the binding of anti-H PL antibodies. One to 3 m M GalNAc inhibited HPL-binding in two out of nine antibodies. None of the antibodies bound in the presence of micrograms per ml of the polyvalent blood group A-substance from hog stomach. Similarly, all anti-HPL antibodies were prevented from binding if non-inhibitory concentrations of A-substance were supplem ented with GalNAc. Lectins from H elix aspersa (HAL) and H elix lucorum (H LL) differed from HPL in antigenic properties. Only one anti-HPL antibody each bound these lectins as well as HPL. Binding of lectins of Cepaea and Rapana was scarcely detectable. Most of the anti-HPL antibodies and the m ultivalent H PL-antigens formed precipitation lines in double diffusion tests. At least two antibodies (IgMs) did so with HLL but none with HAL. The possibility that antibodies were selected because of unknown interactions between HPL and the carbohydrate moieties of certain fractions of antibodies was excluded by raising the antibodies in the presence of tunicamycin to inhibit N-glycosylation.

scholarly journals Human and Mouse Monoclonal Antibodies to Blood Group A Substance, Which Are Nearly Identical Immunochemically, Use Radically Different Primary Sequences

1995 ◽  
Vol 270 (21) ◽  
pp. 12457-12465 ◽  
Author(s):  
Katherine G. Nickerson ◽  
Mi-Hua Tao ◽  
Hua-Tang Chen ◽  
James Larrick ◽  
Elvin A. Kabat
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Blood Group A ◽  
Group A ◽  
Human And Mouse

scholarly journals Structural characterization of neutral oligosaccharides with blood-group A and H activity isolated from bovine submaxillary mucin

1991 ◽  
Vol 279 (1) ◽  
pp. 95-103 ◽  
Author(s):  
A V Savage ◽  
S M D'Arcy ◽  
C M Donoghue
Keyword(s):  
Blood Group ◽  
Methylation Analysis ◽  
Molar Ratios ◽  
Blood Group A ◽  
Group A ◽  
Bovine Submaxillary Mucin ◽  
Type 3 ◽  
Blood Group H

In this study we investigated the structures of 11 neutral oligosaccharides released from bovine submaxillary mucin by alkaline borohydride treatment and isolated by h.p.l.c. One hexa-, one penta-, three tetra-, four tri- and two di-saccharides containing core types 1, 2, 3 or 4 were obtained. We report their structures, determined by a combination of one- and two-dimensional 1H n.m.r. spectroscopy at 270 MHz and methylation analysis involving g.l.c.-m.s., along with their approximate molar ratios. Only three of these oligosaccharides have previously been reported in this source. Of the new oligosaccharides, one contains the blood-group-A antigenic determinant, two contain the blood-group-H type 2 determinant, while another contains the blood-group-H type 3 determinant. The oligosaccharide GlcNAc beta (1→6)[GlcNAc beta (1→3)]GalNAcol, although previously found as a core structure, has been isolated here as a novel trisaccharide.

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