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Titolo:
AFFINITY-PURIFIED ANTIBODIES AGAINST ALPHA-GALACTOSYL RESIDUES FROM HUMAN SERUM - COMPARISON OF THEIR BINDING IN BOVINE TESTICULAR TISSUE WITH THAT OF THE GRIFFONIA-SIMPLICIFOLIA LECTIN (GSI-B-4) AND IMPACT OFLABELING ON EPITOPE LOCALIZATION
Autore:
DONG X; AMSELGRUBER WM; KALTNER H; GABIUS HJ; SINOWATZ F;
Indirizzi:
UNIV MUNICH,FAK TIERARZTLICHE,INST TIERANAT,VET STR 13 D-80539 MUNICHGERMANY UNIV MUNICH,FAK TIERARZTLICHE,INST TIERANAT D-80539 MUNICH GERMANY UNIV MUNICH,FAK TIERARZTLICHE,INST PHYSIOL CHEM D-80539 MUNICH GERMANY
Titolo Testata:
European journal of cell biology
fascicolo: 1, volume: 68, anno: 1995,
pagine: 96 - 101
SICI:
0171-9335(1995)68:1<96:AAAARF>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL; IGG; GAL; HISTOCHEMISTRY; MACROPHAGES; PROTEINS; SPERM; TOOL;
Keywords:
LECTIN; IMMUNOGLOBULIN; GLYCOCONJUGATES; HISTOCHEMISTRY; AFFINITY CHROMATOGRAPHY; TESTES; SPERMATOZOA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
X. Dong et al., "AFFINITY-PURIFIED ANTIBODIES AGAINST ALPHA-GALACTOSYL RESIDUES FROM HUMAN SERUM - COMPARISON OF THEIR BINDING IN BOVINE TESTICULAR TISSUE WITH THAT OF THE GRIFFONIA-SIMPLICIFOLIA LECTIN (GSI-B-4) AND IMPACT OFLABELING ON EPITOPE LOCALIZATION", European journal of cell biology, 68(1), 1995, pp. 96-101

Abstract

alpha-Galactosyl residues in the carbohydrate part of cellular glycoconjugates can serve as cell type-associated markers and are implicatedin intercellular adhesion and biosignaling. This biological significance explains the interest to characterize probes with respective specificity as the Griffonia simplicifolia I-isolectin B-4. Due to the documented occurrence of an alpha-galactoside-binding immunoglobulin G fraction in human serum we compared the extent of binding and its patternfor the lectin and the antibody using surface-immobilized extract proteins and fixed sections of bovine testicular tissue with known lectinreactivity. The antibody fractions were obtained either solely from affinity chromatography isolation on immobilized melibiose or after an additional step to deplete this fraction of galactoside-binding activities without pronounced specificity to the alpha-anomeric linkage. They yielded a rather indistinguishable reactivity in comparison to that of the lectin, when an indirect approach was used. Labeling of the antibodies with a hydrazide derivative of biotin did not affect the pattern of binding. However, significant differences were noted, when conjugation of label was targeted to amino groups via N-hydroxy-succinimideesters of biotin and digoxigenin despite performance of the modification under activity-preserving conditions. Notably, the apparent strongstaining of Leydig cells and nuclei of primary spermatocytes, respectively was not inhibitable by sugar. These differences were corroborated by a nonidentical response of the various probes in solid-phase assays with extract proteins. Thus, care should be exercised in the interpretation of histochemical data, obtained with this type of modified antibody. When these precautions are fulfilled, this immunoglobulin fraction from human serum has the potential as an alpha-galactosyl-specific histochemical tool.

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Documento generato il 04/12/20 alle ore 22:30:08