Studies on equine transferrin—I. The isolation and partial characterization of the D and R variants

Chung, Maxey C.M.; McKenzie, H.A.

doi:10.1016/0305-0491(85)90209-3

Cited by 8 publications

(5 citation statements)

References 15 publications

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“…Preliminary work has been mainly focused on recognizing and identifying different TF variants (Maeda, McKenzie and Shaw, 1984;Chung and Mckenzie, 1985). For instance, a number of genetic variants of human TF have been characterized and their electrophoretic variation confirmed to result from a single amino acid (aa) substitution (Welch and Langmead, 1990).…”

Section: Introductionmentioning

confidence: 99%

Molecular Basis of Transferrin Polymorphism in Goldfish (Carassius auratus)

2004

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Transferrin (TF) polymorphism was investigated in a color variety of goldfish (Carassius auratus), and its molecular basis analyzed. Three TF variants (A 1 , A 2 and B 1 ) were identified from an inbred strain of the goldfish, of which A 1 and B 1 displayed a large electrophoretic difference on both native and SDS-PAGE gels. The TF cDNAs corresponding to variants A 1 and B 1 were cloned and sequenced from A 1 A 1 , A 1 B 1 and B 1 B 1 individuals, and their deduced amino acid sequences were analyzed. Substantial amino acid variation occurred between variants A 1 and B 1 , with significant differences in peptide length, theoretical molecular weight (Mw) and isoelectric point (pI). No potential glycosylation sites were observed in the two amino acid sequences, which excluded the possibility that carbohydrate difference might cause electrophoretic variation among the TF variants. Further analysis suggested that the distinct electrophoretic mobility of the two variants A 1 and B 1 by SDS-PAGE resulted from their Mw difference, while the difference by the native PAGE could be explained by their pI variation. Furthermore, genomic DNA fragments containing the transferrin alleles were amplified and subjected to RFLP analysis in A 1 A 1 , A 1 B 1 and B 1 B 1 individuals. The data revealed characteristic banding patterns for each TF genotype, and demonstrated that the TF alleles A 1 and B 1 could be used as a co-dominant marker system. The initial work relating to the goldfish TF variants will benefit the understanding of the evolutionary and functional significance of TF polymorphism in fish.

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Section: Introductionmentioning

confidence: 99%

Molecular Basis of Transferrin Polymorphism in Goldfish (Carassius auratus)

2004

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“…In the D2 (= C) variant, the two zones have equal staining intensity (Stratil & Glasnák 1981). In some variants that have been studied (C = D2, D, O, R) the main anodal component has four sialic acid residues, while the cathodal component has two residues (Stratil & Glasnák 1981;Stratil et al 1984;Chung & McKenzie 1985;Coddeville et al 1989). This may also apply to other variants.…”

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confidence: 97%

“…Each variant, except D2 (= C), has a typical electrophoretic pattern consisting of two main zones, the anodal one being stronger. In some variants that have been studied (C = D2, D, O, R) the main anodal component has four sialic acid residues, while the cathodal component has two residues (Stratil & Glasnák 1981;Stratil et al 1984;Chung & McKenzie 1985;Coddeville et al 1989). In some variants that have been studied (C = D2, D, O, R) the main anodal component has four sialic acid residues, while the cathodal component has two residues (Stratil & Glasnák 1981;Stratil et al 1984;Chung & McKenzie 1985;Coddeville et al 1989).…”

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confidence: 99%

A partially deficient and atypical equine transferrin variant, TF N

Niini¹,

Stratil

Čižová-Schröffelová

et al. 1997

Animal Genetics

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A new, partially deficient and phenotypically atypical transferrin variant, TF N, was detected in sera of a number of Finnhorses belonging to one family. The variant was inherited codominantly. In polyacrylamide gel electrophoresis (pH 9.0) of sera, variant N appeared as a single weak band migrating slightly faster than the main anodal band of variant M. After immunoblotting or isolation an additional, still weaker, faster band was observed as well as some trace bands. The cathodal component, which is present in other transferrin variants, could not be convincingly proved. The main component of variant N contained four sialic acid residues.

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“…2,6,12,16,17 The horse has more than 15 known variants of transferrin. 3,4,6,9,13 Variation in horse transferrin may be the result of evolutionary selection; specifically, as bacteria evolved the capacity to obtain iron from transferrin, the horse evolved new variants of transferrin to resist these bacteria.…”

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confidence: 99%

Rhodococcus Equi and Genetic Susceptibility: Assessing Transferrin Genotypes from Paraffin-Embedded Tissues

et al. 2003

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Abstract. Rhodococcus equi is a bacterial pathogen, ubiquitous in the soil, that infects many foals and is lethal to some. Transferrin is an iron-binding protein that has bacteriostatic properties in the blood. Transferrin is also highly polymorphic in most species, with 15 variants identified for horses using biochemical methods, and may be responsible for variation in susceptibility to bacterial pathogens. The objectives of this study were 1) to compare biochemical typing with DNA typing of transferrin, 2) to determine if transferrin DNA from archival paraffin-embedded tissue samples can be recovered and typed with molecular methods, and 3) to determine if there was an association between foal death caused by R. equi and transferrin type. Comparing biochemical methods and DNA sequencing for 41 horses demonstrated correspondence between the typing methods. The allele frequency of archival paraffin-embedded tissue samples from 34 Thoroughbred foals that succumbed to R. equi showed an excess of the F allele and a deficiency of the D allele (P Ͻ 0.05). Year of collection (P Ͼ 0.8), age of foal (P Ͼ 0.3), and sex of foal (P Ͼ 0.6) were not statistically associated with transferrin type. The archival material was successfully transferrin typed using DNA sequencing, and there may be an association between foal death caused by R. equi and transferrin type.

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Studies on equine transferrin—I. The isolation and partial characterization of the D and R variants

Cited by 8 publications

References 15 publications

Molecular Basis of Transferrin Polymorphism in Goldfish (Carassius auratus)

Molecular Basis of Transferrin Polymorphism in Goldfish (Carassius auratus)

A partially deficient and atypical equine transferrin variant, TF N

Rhodococcus Equi and Genetic Susceptibility: Assessing Transferrin Genotypes from Paraffin-Embedded Tissues

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