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  • 1
    ISSN: 1432-0428
    Keywords: Diabetic rats ; wheat germ agglutinin ; N-acetyl glucosamine ; glomerular basement membrane ; lectin histochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary This study was designed to establish whether specific early changes in carbohydrate content of proteins in the glomerulus of the diabetic rat could be detected. Lectin staining of kidney sections from streptozotocin-induced diabetic rats were compared with similar sections from healthy and diabetic rats that were treated with insulin. Animal groups were killed 1 month, 3 months and 6 months after induction of diabetes. There were no differences in the staining of the glomerular basement membrane between control, insulin-treated and diabetic rats for the lectins concanavalin A, lotus tetragonolobus, soybean and kidney bean, with and without trypsinisation. Staining of the glomerulur basement membrane with wheat germ agglutinin after trypsinisation was significantly increased in the diabetic group when compared to both healthy and insulin-treated groups (p 〈 0.01). It was concluded that, in experimental diabetes mellitus in the rat, there is an accumulation of substances in the glomerular basement membrane and mesangium with an affinity for wheat germ agglutinin, most probably N-acetyl glucosamine, and this is partially prevented by insulin treatment.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0983
    Keywords: Aspergillus ; Neurospora ; Isocitrate lyase ; Glyoxysome ; Acetate metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequences of the genes encoding the acetate-inducible glyoxylate cycle enzyme isocitrate lyase from the ascomycete fungi Aspergillus nidulans (acuD) and Neurospora crassa (acu-3) are presented. The respective A. nidulans and N. crassa genes are interrupted at identical positions by two introns and encode proteins of 538 and 543 amino acids, which have 75% identity. The predicted protein sequences do not demonstrate the C-terminal tripeptide S-K-L that has been implicated in peroxisomal targeting and found in the glyoxysomally located enzyme malate synthase from the same species. However, the protein sequences do exhibit a partial repeat which, in common with malate synthase, is located in regions that are absent from, or non-homologous with, the E. coli enzyme, which is not compartmentalized.
    Type of Medium: Electronic Resource
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