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  • 1
    ISSN: 1432-2048
    Keywords: Arabinogalactan-protein ; Immunolocalization ; Plasma membrane ; Protoplast surface ; Raphanus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rabbit antisera were raised against β-(1→6)-galactotetraose coupled to bovine serum albumin (Gal4-BSA). The antisera reacted with arabinogalactan-proteins (AGPs) isolated from seeds, roots, or leaves of radish (Raphanus sativus L.) as revealed by immunodiffusion analysis. Extensive removal of α-l-arabinofuranosyl residues from these AGPs enhanced the formation of precipitin with the antisera. The antisera did not react with such other polysaccharides as soybean arabinan-4-galactan, β-(1→4)-galactan, and β-(1→3)-galactan, indicating their high specificity toward the consecutive β-(1→6)-galactosyl side chains of AGPs. The antibodies were purified by affinity chromatography on a column of immobilized β-(1→6)-galactotetraose as ligand. The specificity of the antibodies toward consecutive (1→6)-linked β-galactosyl residues was confirmed by enzyme-linked immunosorbent assay for hapten inhibition against Gal4-BSA as antigen, which revealed that β-(1→6)-galactotriose and-tetraose were potent inhibitors, while β-(1→3)-or β-(1→4)-galactobioses and -trioses were essentially unreactive. Electron-microscopic observation of immunogold-stained tissues demonstrated that AGPs were localized in the middle lamella as well as at the plasma membrane of primary roots of radish. Agglutination of protoplasts prepared from cotyledons occurred with the antibodies, supporting the evidence for localization of AGPs in the plasma membrane. The antibody-mediated agglutination was inhibited by addition of AGPs or β-(1→6)-galactotetraose.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0428
    Keywords: Apolipoprotein(a) ; diabetes mellitus ; family study ; lipids ; lipoprotein(a) ; lipoproteins ; phenotypes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We studied the quantitative and qualitative characteristics of lipoprotein(a) [Lp(a)] as a function of apolipoprotein(a) [apo(a)] phenotype in 87 members (42 males, 45 females) of 20 diabetic families, 26 of whom were diagnosed with non-insulin-dependent diabetes mellitus (NIDDM) with moderate glycaemic control (HbA1c7.1±1.2%). Apo(a) phenotyping was performed by a sensitive, high-resolution technique using SDS-agarose/gradient PAGE (3–6%). To date, 26 different apo(a) phenotypes, including a null type, have been identified. Serum Lp(a) levels of NIDDM patients and non-diabetic members of the same family who had the same apo(a) phenotypes were compared, while case control subjects were chosen from high-Lp(a) non-diabetic and low-Lp(a) non-diabetic groups with the same apo(a) phenotypes in the same family. Serum Lp(a) levels were significantly higher in NIDDM patients than in non-diabetic subjects (39.8±33.3 vs 22.3±19.5 mg/dl, p〈0.05). The difference in the mean Lp(a) level between the diabetic and non-diabetic groups was significantly (p〈0.05) greater than that between the high-Lp(a) non-diabetic and low-Lp(a) non-diabetic groups. An analysis of covariance and a least square means comparison indicated that the regression line between serum Lp(a) levels [log Lp(a)] and apo(a) phenotypes in the diabetic patient group was significantly (p〈0.01) elevated for each apo(a) phenotype, compared to the regression line of the control group. These data, together with our previous findings that serum Lp(a) levels are genetically controlled by apo(a) phenotypes, suggest that Lp(a) levels in diabetic patients are not regulated by smaller apo(a) isoforms, and that serum Lp(a) levels are greater in diabetic patients than in non-diabetic family members, even when they share the same apo(a) phenotypes.
    Type of Medium: Electronic Resource
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