Displaying all 4 publications

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  1. Saha N
    Ann Hum Biol, 1987 7 1;14(4):349-56.
    PMID: 3662433
    The distribution of serum transferrin subtypes was determined by PAG electrophoresis and isoelectric focussing in a group of 2288 individuals from 10 Mongoloid populations of East Asia. The sample comprised 857 Chinese from different localities: Singapore (239), Malaysia (228), Taiwan (265), Hong Kong (65), Fouzhou (60); Koreans (332), Filipinos (281), Thais (455), Malays (335) and Indonesians (28). The frequencies of TfC1 varied from 0.73 to 0.79 in the Chinese and from 0.76 to 0.83 in the other Mongoloid populations. TfC3 was observed at a frequency of 0.02 in the Koreans and Chinese from Fouzhou. TfDChi was present in a low frequency (0.01 to 0.03) in all the populations. A low frequency of TfB was also present in all the populations. The phenotypic distribution of transferrin subtypes was at Hardy-Weinberg equilibrium in all the populations.
    Matched MeSH terms: Transferrin/genetics*
  2. Tan SG, Teng YS, Ganesan J, Lau KY, Lie-Injo LE
    Hum Genet, 1979 Jul 18;49(3):349-53.
    PMID: 289626
    Kadazans, the largest indigenous group in Sabah, northern Borneo, were surveyed for glyoxalase I, phosphoglucomutase I, red cell acid phosphatase, esterase D, adenosine deaminase, soluble glutamate pyruvate transaminase, soluble glutamate oxaloacetate transaminase, 6-phosphogluconate dehydrogenase, uridine monophosphate kinase, adenylate kinase, peptidase B and D, superoxide dismutase, C5, group specific component, haptoglobin and transferrin. Kadazans were found to be polymorphic for GLO I, PGM I, RCAP, esterase D, ADA, s-Gpt, 6PGD, UMPK, Gc, C5, haptoglobin and peptidase B. Rare variants were found for transferrin and peptidase D. No variant was found for s-Got, SOD and AK.
    Matched MeSH terms: Transferrin/genetics
  3. Tan SG, Gan YY, Asuan K
    Hum Genet, 1982;60(4):369-70.
    PMID: 7106773
    Malays, Chinese, and Indians from Peninsular Malaysia; Ibans and Bidayuh from Sarawak State; Kadazans from Sabah State, Northern Borneo; and Bataks, Minangkabau, and Javanese from North Sumatra, Indonesia, were subtyped for transferrin C by polyacrylamide gel isoelectric focusing. All nine populations studied are polymorphic for two alleles, TfCl and TfC2, TfC3 was polymorphic in six populations and present as a rare variant in the other three. The frequency of TfC1 ranged from 0.855 in Bidayuh to 0.711 in Javanese, that of TfC2 from 0.231 in Indians to 0.113 in Bidayuh, and that of TfC3 from 0.030 in Javanese and Chinese to 0.008 in Bidayuh. TfDchi is polymorphic in all the populations that we studied except in Minangkabau, in whom it is present as a rare variant, and in Indians, in whom it is absent.
    Matched MeSH terms: Transferrin/genetics*
  4. Mohd-Padil H, Mohd-Adnan A, Gabaldón T
    Mol Biol Evol, 2013 Apr;30(4):894-905.
    PMID: 23258311 DOI: 10.1093/molbev/mss325
    Transferrin is a protein super-family involved in iron transport, a central process in cellular homeostasis. Throughout the evolution of vertebrates, transferrin members have diversified into distinct subfamilies including serotransferrin, ovotransferrin, lactoferrin, melanotransferrin, the inhibitor of carbonic anhydrase, pacifastin, and the major yolk protein in sea urchin. Previous phylogenetic analyses have established the branching order of the diverse transferrin subfamilies but were mostly focused on the transferrin repertoire present in mammals. Here, we conduct a comprehensive phylogenetic analysis of transferrin protein sequences in sequenced vertebrates, placing a special focus on the less-studied nonmammalian vertebrates. Our analyses uncover a novel transferrin clade present across fish, sauropsid, and amphibian genomes but strikingly absent from mammals. Our reconstructed scenario implies that this novel class emerged through a duplication event at the vertebrate ancestor, and that it was subsequently lost in the lineage leading to mammals. We detect footprints of accelerated evolution following the duplication event, which suggest positive selection and early functional divergence of this novel clade. Interestingly, the loss of this novel class of transferrin in mammals coincided with the divergence by duplication of lactoferrin and serotransferrin in this lineage. Altogether, our results provide novel insights on the evolution of iron-binding proteins in the various vertebrate groups.
    Matched MeSH terms: Transferrin/genetics*
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