The Relationship of the H Substance to the A–B–O Blood Groups

Wiener, A.S.; Moor‐Jankowski, J.; Gordon, Eve B.

doi:10.1159/000229689

Cited by 41 publications

(32 citation statements)

References 13 publications

(14 reference statements)

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“…Former studies on human isohcmaglutinins indicate that these may be subdivided into two broad categories. One category, obtained from occasional individuals of subgroup AXB, is designated as anti-H, and is a weak cold agglutinin paralleling in specificity the anti-H lectins, for example, the Ulex europeus [13] lectin. The second, contrasting category of isoagglutinins is designated as anti-C; it occurs in group O scrum and reacts with red cells of groups A and B but not of group O.…”

Section: Discussionmentioning

confidence: 99%

The Specificity of Hemagglutinating Bean and Seed Extracts (Lectins)

Wiener¹,

Moor‐Jankowski²,

Gordon³

1969

Int Arch Allergy Immunol

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Section: Discussionmentioning

confidence: 99%

The Specificity of Hemagglutinating Bean and Seed Extracts (Lectins)

Wiener¹,

Moor‐Jankowski²,

Gordon³

1969

Int Arch Allergy Immunol

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“…The Rh system was mistakenly named after the rhesus monkey due to confusion with the LW antigen (named after Landsteiner and Wiener), but erythrocytes from neither the rhesus monkey, other nonhuman primates, nor any other mammalian species contain the Rh antigens (18). Chimpanzees have a blood group system with similarities to Rh (19), but the serologically defined surface Rh epitope has undoubtedly diverged extensively between species, for considerable divergence exists even between Rh positive and negative humans. Nevertheless, ifthe core Rh polypeptides are ofgeneral importance to erythrocyte membranes, existence in diverse species should be expected.…”

Section: Introductionmentioning

confidence: 99%

Isolation of proteins related to the Rh polypeptides from nonhuman erythrocytes.

Saboori¹,

Denker²,

Agre³

1989

J. Clin. Invest.

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It is thought that the Rh antigens may be important in maintaining normal erythocyte membrane integrity. Despite their name, Rh antigens are serologically present only on human erythrocytes. Rh structural polymorphisms are known to reside within a family of nonglycosylated M, 32,000 integral membrane proteins that can be purified by hydroxylapatite chromatography. M, 32,000 integral membrane proteins were purified similarly from erythrocyte membrane vesicles prepared from rhesus monkeys, cows, cats, and rats, but could not be purified from human Rhw erythrocytes, a rare syndrome lacking Rh antigens. The purified M, 32,000 polypeptides were labeled with 1251, digested with chymotrypsin, and found to be 30-60% identical to human Rh polypeptides when compared by two-dimensional iodopeptide mapping. The physiologic function of the Rh polypeptides remains to be identified; however, the existence of related proteins in nonhuman erythrocytes supports the concept that the Rh polypeptides are erythrocyte membrane components of fundamental significance.

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“…However, Solomon et al [13] proposed an alternative pathway for the development of A in the absence of H in their Ahm blood and this theory was supported and extended by the studies of Wiener et al [20].…”

Section: Discussionmentioning

confidence: 93%

“…The aim of this paper is to show that only the alternative pathway, as proposed by Solomon et al [13] and supported by Wiener et al [20] is necessary for the formation of the first formed parts of the A mosaic as present in A2 cord and adult A2B bloods ; whereas those parts of A that react with Dolichos bif. anti-A and which are formed later in the biosynthetic pathway [14] utilise H in their development in accordance with the orthodox pathway proposed by Watkins and Morgan [18] and Ceppellini [3].…”

mentioning

confidence: 84%

The Role of H in the Development of A

Voak¹,

Lodge²

1968

Vox Sanguinis

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A(2) cord bloods do not react with Dolichos bif. anti-A and their H status is equivalent to that of group O cord bloods, indicating that the A components of these bloods are formed independently of H. Bloods reacting with Dolichos bif. extract require H for the development of their A(1) components and this is reflected in the lower H status of these bloods. As the alternative pathway is necessary for the development of the first formed parts of A both the alternative and the orthodox pathways are necessary for the development of bloods with A(1) components.

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The Relationship of the H Substance to the A–B–O Blood Groups

Cited by 41 publications

References 13 publications

The Specificity of Hemagglutinating Bean and Seed Extracts (Lectins)

The Specificity of Hemagglutinating Bean and Seed Extracts (Lectins)

Isolation of proteins related to the Rh polypeptides from nonhuman erythrocytes.

The Role of H in the Development of A

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