Výsledky vyhledávání - "A. L. Tárnoky"

Genetic variants showing apparent hot-spots in the human serum albumin gene

Autor: John C Chapman, Lorenzo Minchiotti, András L Tárnoky, Ulrich Kragh-Hansen, Monica Galliano, Monica Campagnoli

Publikováno v: Clinica Chimica Acta. 289:45-55

The molecular defects of three different slow-migrating genetic variants of human serum albumin, albumins Kamloops (formerly RIH), Stirling and Amsterdam, previously characterized only by electrophoretic and dye-binding studies, are now reported. Two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb5c32840ab125330585020c3b1b6d94
https://doi.org/10.1016/s0009-8981(99)00166-7

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Effect of genetic variation on the fatty acid-binding properties of human serum albumin and proalbumin

Autor: Monica Galliano, Francisco M. Salzano, Maria Helena Pereira Franco, Lorenzo Minchiotti, Henning Nielsen, András L Tárnoky, Stephen O. Brennan, Osamu Sugita, Ulrich Kragh-Hansen

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1342:191-204

In the circulation, non-esterified fatty acids are transported by albumin which also facilitates their removal from donor cells and uptake into receptor cells. We have studied whether genetic variations in the albumin molecule can affect its in vivo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9b09d268cd3b5bafac8848397edd2d8
https://doi.org/10.1016/s0167-4838(97)00099-x

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Genetic variation in human serum albumin: a 313 Lys--Asn mutation in albumin reading identified by PCR analysis

Autor: Lorenzo Minchiotti, András L Tárnoky, Monica Galliano, Demetris Savva, Ulrich Kragh-Hansen, Bing Li

Publikováno v: Clinica chimica acta; international journal of clinical chemistry. 270(2)

An early case of bisalbuminaemia was reported in this journal in 1964, with the name Albumin Reading added later. Its use in electrophoretic comparisons led to some new variants being described as 'of the Reading type' on this basis alone. Protein se

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc6bd783819e648526518be7eb4bf10f
https://pubmed.ncbi.nlm.nih.gov/9544457

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High-affinity binding of laurate to naturally occurring mutants of human serum albumin and proalbumin

Autor: Ulrich Kragh-Hansen, Maria Helena Pereira Franco, Francisco M. Salzano, Stephen O. Brennan, Anders Overgaard Pedersen, Monica Galliano, Lorenzo Minchiotti, András L Tárnoky

Publikováno v: The Biochemical journal. 320

Binding of laurate (n-dodecanoate) to genetic variants of albumin or its proprotein and to normal albumin isolated from the same heterozygous carriers was studied by a kinetic dialysis technique at physiological pH. The first stoichiometric associati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70c55d1cd307d856d3d21a9825a9b80a
https://pubmed.ncbi.nlm.nih.gov/9003380

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Genetic variants of serum albumin: a study of albumin Kashmir

Autor: A L, Tárnoky, M F, Vickers, D, Savva

Publikováno v: Indian journal of biochemistrybiophysics. 29(5)

The study of human serum albumin variants is reviewed with reference to albumin Kashmir, a typical variant. Its published instances are listed and its position in this field of investigations is indicated.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::df2fbd0401301a48835e967d6682841d
https://pubmed.ncbi.nlm.nih.gov/1289226

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Genetic characterization of an alloalbumin, albumin Kashmir, using gene amplification and allele-specific oligonucleotides

Autor: D, Savva, A L, Tárnoky, M F, Vickers

Publikováno v: The Biochemical journal. 266(2)

The molecular basis for albumin Kashmir was studied using the polymerase chain reaction to amplify a DNA fragment containing codon 501 in exon 12 of the human albumin gene. Southern blots of the amplified DNA were hybridized to oligonucleotide probes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::be1f1dead55d6dc24c62acde27ad1a90
https://pubmed.ncbi.nlm.nih.gov/2317208

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