scholarly journals Immunochemical studies on blood groups LXVI. Competitive binding assays of A1 and A2 blood group substances with insolubilized anti-A serum and insolubilized A agglutinin from Dolichos biflorus.

1978 ◽  
Vol 147 (3) ◽  
pp. 830-843 ◽  
Author(s):  
E C Kisailus ◽  
E A Kabat
Keyword(s):  
Blood Group ◽  
Competitive Binding ◽  
Binding Assays ◽  
Dolichos Biflorus ◽  
Group A ◽  
Blood Group Substances ◽  
Lower Slope ◽  
Competitive Binding Assays

Competitive binding assays using 3H-labeled blood group A substance and insolubilized Dolichos biflorus lectin or human anti-A were carried out, measuring competition by blood group A1 and A2 glycoproteins, and by unabsorbed anti-A sera, and with these sera absorbed with the A1 and A2 glycoproteins. With Dolichos lectin specific for (formula: see text) A1 substances had about 11 times as many determinants as did A2 substances, but the slopes of the lines in the competitive binding assays were the same. With insolubilized anti-A, A2 substances gave lines of lower slopes. Although individual A1 populations varied in the amounts giving 50% inhibition in the assays, as did A2 substances, the slopes of the lines for the A1 substances were the same and always higher than the slopes of the lines for the A2 substances. Competitive binding assays with unabsorbed anti-A sera and with these sera absorbed with insoluble polyleucyl A1 and A2 substances showed that partial absorption of polyleucyl A1 substances left antibodies of lower slope in the supernate, whereas absorption with polyleucyl A2 substance left antibodies (anti-A1) having the same or an even higher slope than the unabsorbed sera. The findings indicate that human A1 and A2 glycoproteins differ in their determinants, and that A2 specificity is determined by the type 2 chain in which the A trisaccharide (formula: see text) is linked beta 1 leads to 4 to DGlcNAc, whereas the A1 specificity is determined by the type 1 chain in which this trisaccharide is linked beta 1 leads to 3 to DGlcNAc; most of the determinants in the glycoproteins have a second LFuc linked alpha 1 leads to 3 and alpha 1 leads to 4 to the DGlcNAc of the type 2 and type 1 chains, respectively.

scholarly journals Immunochemical studies on blood groups LXII. Fractionation of hog and human A, H, and AH blood group active substance on insoluble immunoadsorbents of Dolichos and Lotus lectins.

1976 ◽  
Vol 143 (2) ◽  
pp. 422-436 ◽  
Author(s):  
M E Pereira ◽  
E A Kabat
Keyword(s):  
Blood Group ◽  
Optical Rotation ◽  
Gastric Mucin ◽  
Specific Optical Rotation ◽  
Dolichos Biflorus ◽  
Blood Group A ◽  
Analytical Properties ◽  
Group Substance ◽  
Group A

The purified lectins from Lotus tetragonolobus and Dolichos biflorus were coupled to Sepharose 2B to make insoluble adsorbents for purification and fractionation of blood group A and H active glycoproteins. With both adsorbents, hog gastric mucin A + H blood substance (HGM), purified by phenol-ethanol precipitation, yielded fractions showing only A, only H, or AH activities. The AH fraction was obtained when the adsorbent column was overloaded with HGM and its A and H specificities seem to be carried on the same molecules since they were not separable by chromatography on either column. However A and H specificities of blood group substance from the stomach of a presumably heterozygous individual hog were both on the same molecules as they too could not be fractionated on either column. Analytical properties of the isolated fractions were generally similar to those of the unfractionated material, the purfied A substances had a higher galactosamine/fucose ratio than did the H substances. Although the original A + H showed very little specific optical rotation, the separated A and H substances rotated positively and negatively, respectively. The lectin-Sepharose adsorbents have also proven useful in isolating A or H substances directly from the crude commercial hog gastric mucin. Blood group A2 substance from a human ovarian cyst yielded two fractions on the Lotus-Sepharose column; the effluent did not interact with the Lotus lectin but precipitated the Ulex and Dolichos lectins and anti-A, and appears to contain type 1 H determinants. The other fraction reacted with Lotus and Ulex lectin as well as with Dolichos and anti-A.

scholarly journals Further studies of oligosaccharide recognition by the soluble 13 kDa lectin of bovine heart muscle. Ability to accommodate the blood-group-H and -B-related sequences

1988 ◽  
Vol 252 (1) ◽  
pp. 283-287 ◽  
Author(s):  
W M Abbott ◽  
E F Hounsell ◽  
T Feizi
Keyword(s):  
Blood Group ◽  
Heart Muscle ◽  
Human Lung ◽  
Distinctive Features ◽  
Bovine Heart ◽  
Group A ◽  
Group B ◽  
Blood Group H

Oligosaccharide recognition by the 13 kDa soluble lectin from bovine heart muscle has been investigated by inhibition of binding of the 125I-labelled lectin to trypsin-treated rabbit erythrocytes. The results indicate that the Type 1 (Gal beta 1-3GlcNAc) and the Type 2 (Gal beta 1-4GlcNAc) backbone structures are the basic recognition units, and that the blood-group-H structure, the blood-group-B structure, the ‘B-like’ structure [afucosyl-(blood group B)] and the alpha 2-3 sialylated analogues of the backbone structures can also be accommodated and hence are candidate receptor structures for the lectin. A comparison of available inhibition data on six other soluble beta-galactoside-binding lectins (three from human lung and three from rat lung) has shown some common features among these and the bovine lectin, e.g. in general a stronger reaction with N-acetyl-lactosamine than with lactose, and a lack of reaction with 3-fucosyl-lactose and 6-sialyl-lactose. However, there are distinctive features among the lectins, e.g. differences in relative reactions with the blood-group-A structure, and no two of the lectins appear to be identical in their fine specificities.

Developmental changes of blood group A-active glycosphingolipids with type 1 and type 2 chains in rat small intestine

1987 ◽  
Vol 4 (1) ◽  
pp. 59-71 ◽  
Author(s):  
Daniele Bouhours ◽  
G�ran Larson ◽  
Jean-Francois Bouhours ◽  
Arne Lundblad ◽  
Gunnar C Hansson
Keyword(s):  
Small Intestine ◽  
Blood Group ◽  
Developmental Changes ◽  
Rat Small Intestine ◽  
Blood Group A ◽  
Group A

Use of Synthetic H Disaccharides as Acceptors for Detecting Activities of UDP-GalNAc:Fuc α1-->2Galβ-R α1-->3-N-Acetylgalactosaminyltransferase in Plasma Samples from Blood Group A Subgroups

1992 ◽  
Vol 38 (12) ◽  
pp. 2392-2395 ◽  
Author(s):  
S Yazawa ◽  
A Takeya ◽  
O Hosomi ◽  
T Nakajima ◽  
N Shimoda ◽  
...  
Keyword(s):  
Human Plasma ◽  
Blood Group ◽  
Enzyme Activities ◽  
Enzyme Concentration ◽  
Plasma Samples ◽  
Blood Group A ◽  
Significant Difference ◽  
Group A

Abstract Concentrations of blood group A-specified alpha(1-->3)-N-acetylgalactosaminyltransferase (A enzyme) were measured in human plasma of blood groups A1, A2, and A3 by using chemically synthesized H disaccharides and H type 1 and type 2 trisaccharides attached to hydrophobic aglycones as acceptors. When the trisaccharides were used as acceptors, enzyme activities were reduced in samples from A2 and A3. However, the H disaccharides were shown to be good acceptors even for enzymes from A2 and A3, and no significant difference in enzyme concentration was detected in any of the plasma tested.

Monoclonal antibodies defining blood group A variants with difucosyl type 1 chain (ALeb) and difucosyl type 2 chain (ALey)

Biochemistry ◽  
1985 ◽  
Vol 24 (22) ◽  
pp. 6190-6194 ◽  
Author(s):  
Henrik Clausen ◽  
John M. McKibbin ◽  
Senitiroh Hakomori
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Blood Group A ◽  
Group A

scholarly journals Comparative binding of bovine, human and rat insulin-like growth factors to membrane receptors and to antibodies against human insulin-like growth factor-1

1986 ◽  
Vol 233 (1) ◽  
pp. 215-221 ◽  
Author(s):  
L C Read ◽  
F J Ballard ◽  
G L Francis ◽  
R C Baxter ◽  
C J Bagley ◽  
...  
Keyword(s):  
Growth Factors ◽  
Polyclonal Antiserum ◽  
Competitive Binding ◽  
Membrane Receptors ◽  
Binding Studies ◽  
Comparative Binding ◽  
Placental Membranes ◽  
Insulin Like Growth Factors

The immunological properties of human, bovine and rat insulin-like growth factors (IGF) and insulin were compared in competitive binding studies with Tr10 and NPA polyclonal antisera raised in rabbits against human IGF-1. Bovine IGF-1 was 11-19% as effective as human IGF-1 in competing for binding with 125I-labelled human IGF-1, whereas IGF-2 reacted poorly and insulin did not compete. Similar competitive binding curves were obtained with the mouse monoclonal anti-(human IGF-1) antibody 3D1, except that bovine IGF-1 showed a severalfold greater affinity for the monoclonal antibody than for either polyclonal antiserum. Membranes isolated from human placenta, sheep placenta and foetal-human liver were used as sources of cellular receptors. In human placental membranes, most of the binding of IGF-1 tracers could be attributed to a type-1 receptor, because insulin inhibited up to 65% of tracer binding. The other two tissues apparently contain only type-2 receptors, as evidenced by the very low potency of bovine or human IGF-1 in competing for binding with IGF-2 tracers and the absence of any competition by insulin. In competition for binding with labelled bovine or human IGF-1 to human placental membranes, bovine IGF-1 had a similar potency to human IGF-1, whereas bovine IGF-1 was more potent in binding studies with tissues rich in type-2 receptors. Rat IGF-2 was considerably less effective than human IGF-2 in competition for receptors on any of the membrane preparations.

scholarly journals The structural and functional features of the microcirculatory bed in patients with arterial hypertension and type 2 diabetes mellitus

2005 ◽  
Vol 11 (3) ◽  
pp. 177-180 ◽  
Author(s):  
L. A. Lohankova ◽  
Yu. V. Kotovskaya ◽  
A. S. Milto ◽  
Zh. D. Kobalava
Keyword(s):  
Diabetes Mellitus ◽  
Blood Flow ◽  
Arterial Hypertension ◽  
Control Group ◽  
Microcirculatory Bed ◽  
Type 2 Dm ◽  
Group A ◽  
Functional Features

The structural and functional features of the microcirculatory heel (MCB) were studied in patients with arterial hypertension (AH) in relation to the presence or absence of type 1 diabetes mellitus (DM). Two hundred and twelve patients were examined. These included 110 patients with grades 1 and 2 arterial hypertension (AH) and type 2 DM, 82 patients with AH without type 2 DM, and 20 apparently healthy individuals. Laser Doppler flowmetry (LDF) was used to estimate basal blood flow, the loading test parameters characterizing the structural and functional status of MCB, and the incidence of hemodynamic types of microcirculation. Patients with AH concurrent with type 1 DM were found to have the following microcirculatory features: an increase in perfusion blood flow (microcirculation index, 8,8±1,8 perf. units versus 4,9±0,8 perf, units in patients with AH without DM and 6,7±0,9 perf. units in the control group), a drastic reduction in myogenic activity to 13,2±5,7 % versus 16,7±6,8 and 25,2±6,4 %, respectively, a decrease in vascular resistance, impairment of autoregulation, and low reserve capacities (reserve capillary blood flow was 197,8±31,6 % versus 429,9±82,01 % in the group of AH without DM and 302,8±50,1 % in the control group), a predominance of the hyperemic hemodynamic type (58,8 % in patients with AH and DM, 20,9 % in those with AH without DM, and 20,0 % in the controls). The specific features of the altered microcirculatory bed in patients with AH concurrent with type 2 DM were ascertained. These included the predominance of hyperemic microcirculation, impaired autoregulation. diminished microvascular resistance, and the low reserve capacities of the microcirculatory bed.

scholarly journals Gambaran Populasi Golongan Darah Subgroup A (A1, A2) di PMI Kulon Progo

Biosfera ◽  
2017 ◽  
Vol 34 (1) ◽  
pp. 47
Author(s):  
Hieronymus Rayi Prasetya ◽  
Bambang Heru Budianto ◽  
Hernayanti Hernayanti
Keyword(s):  
Genetic Variation ◽  
Blood Group ◽  
Sampling Technique ◽  
Red Cross ◽  
Cross Sectional ◽  
Dolichos Biflorus ◽  
Blood Group A ◽  
Group A ◽  
Transfusion Reactions

Subgroup A1 and A2 are the most important in the blood group A. Subgroup A1 has the A antigen more than A2 subgroup, the A2 subgroup can cause misidentification of blood group due to poor A antigen and genetic variation possessed. Misidentification of the blood group will increase the risk of transfusion reactions. This research aims to describe the A1 and A2 subgroup population in Kulon Progo district. This study was conducted with a cross sectional sampling technique. The sample in this study were taken from donors of blood group A in Kulon Progo Red Cross. Identification of A1 and A2 subgroup is done by using lectin (Dolichos biflorus extract). The result of the examination of 53 samples showed that 96,2% was A1 subgroup and 3,8% was A2 subgroup.Key words : Subgroup A1, Subgroup A2, Population, Kulon Progo

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