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Urinary Glycosaminoglycan Electrophoresis With Optimized Keratan Sulfate Separation Using Peltier Sy
26.10.2015 in Journal of Inborn Errors of Metabolism &Screening
The purpose of this communication is to indicate a simple and rapid method with a small volume of urine sample to detect urine glycosaminoglycan (GAG) and serve as a screening procedure for mucopolysaccharidoses (MPSs). Total GAG measurement forpatients with MPS disorders is considered to be the first step indiagnosis of those heterogeneous group of lysosomal storage disorders presenting clinical phenotype. In this study, modified 9-dimethylmethylene blue method is used for total GAG measurement. Following GAG quantitation, the procedure described here allows GAG isolation from a very a small volume of urine sample and subjected to high-resolution GAG electrophoresis, which can be easily performed in routine clinical diagnostic laboratories. Glycosaminoglycan precipitation is a modified method based on total GAG concentration in the urine. For optimizedisolation of total GAG for electrophoresis, instead of considering the urine creatinine concentration, 300μg/mL GAG containing urine is considered to be the target concentration for the best precipitation with 1000 μL cetylpyridinium chloride (CPC)/citratebuffer. Glycosaminoglycan concentration-based precipitation of urine with CP Callowsthelaboratorytobeabletoworkwithasmall volume of urine sample by keeping the precipitating ratio with CPC constant for samples that contain GAG less than 300 μg/mL. Based on the effect of cold buffer using low voltage, GAGs high-resolution electrophoresis banding patterns described here enable aclear separation of keratan sulfate from chondroitin sulfate as well as dermatan sulfate (DS1 and DS2) and heparan sulfate. By this procedure, GAG patterns are more clear, easily identified, and provide a guide for the enzyme analysis deficient in the MPS disorders.
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Mihriban Tijen Tanyalcin, MD, PhD

OPTIMISATION OF KERATAN SULFATE SEPARATION BY USING PELTIER SYSTEM
2-5 September 2014 in Innsbruck

OPTIMISATION OF KERATAN SULFATE SEPARATION BY USING PELTIER SYSTEM FOLLOWING AN IMPROVED RAPID ISOLATION OF URINARY GLYCOSAMINOGLYCANS OFSMALL VOLUME OF URINE SAMPLES

AIM :The procedure described here allows GAG isolation and high resolution  GAG electrophoresis to be easily performed in routine clinical diagnostic laboratories.

Tanyalcin MT Journal of Inborn Errors of Metabolism and Screening, 13th International Symposium on Mucopolysaccharidoses and Related Diseases, Special Supplement With The Abstracts, page 30 August 2014

Tanyalcin T Journal of Inherited Metabolic Disease, Volume 37,  Supplement 1, pp 335  September 2014

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RAPID ANALYSIS OF L-ARGININOSUCCINIC ACID (ASA) BY USING A SHORT PROGRAM OF TOTAL HOMOCYSTEINE
2-5 September 2014 in Innsbruck

AIM :This study presents a rapid quantification of ASA by the modified method of total homocysteine program  for the Norleucine users as an internal standard for full - standard amioacid chromatogram on Biochrom 30 aminoacid analyser.


Tanyalçin T Journal of Inherited Metabolic Disease, Volume 37Supplement 1, pp 158  September 2014

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Mutations in BTD gene causing biotinidase deficiency: a regional report
Kasım 2014

J Pediatr Endocrinol Metab. 2015 Mar 1;28(3-4):421-4. doi: 10.1515/jpem-2014-0056.

Abstract Biotinidase deficiency is an autosomal recessive inborn error of biotin metabolism. Children with biotinidase deficiency cannot cleave biocytin and, therefore, cannot recycle biotin. Untreated individuals become secondarily biotin deficient, which in turn results in decreased activities of the biotin-dependent carboxylases and the subsequent accumulation of toxic metabolites causing clinical symptoms. Biotinidase deficiency is characterized by neurological, cutaneous manifestations and metabolic abnormalities. The worldwide incidence of profound biotinidase deficiency has been estimated at 1:112,271. The human biotinidase gene is located on chromosome 3p25 and consists of four exons with a total length of 1629 base pairs. To date, more than 100 mutations in the biotinidase gene known to cause biotinidase deficiency have been reported. The vast majority of mutations are homozygous or compound heterozygous. Finding known mutations can be correlated with the biochemical enzymatic results. This report summarizes the demographic features of patients identified as biotinidase deficient from August of 2012 through August of 2013 and mutation analysis results for 20 cases in the southeast region of Turkey.

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Enhanced interpretation of newborn screening results without analyte cutoff values.
2012 Jul

Genet Med. 2012 Jul;14(7):648-55. doi: 10.1038/gim.2012.2. Epub 2012 Feb 16.

Marquardt G, Currier R, McHugh DM, Gavrilov D, Magera MJ, Matern D, Oglesbee D, Raymond K, Rinaldo P, Smith EH, Tortorelli S, Turgeon CT, Lorey F, Wilcken B, Wiley V, Greed LC, Lewis B,Boemer F, Schoos R, Marie S, Vincent MF, Sica YC, Domingos MT, Al-Thihli K, Sinclair G, Al-Dirbashi OY, Chakraborty P, Dymerski M, Porter C, Manning A, Seashore MR, Quesada J, Reuben A,Chrastina P, Hornik P, Atef Mandour I, Atty Sharaf SA, Bodamer O, Dy B, Torres J, Zori R, Cheillan D, Vianey-Saban C, Ludvigson D, Stembridge A, Bonham J, Downing M, Dotsikas Y, Loukas YL,Papakonstantinou V, Zacharioudakis GS, Baráth A, Karg E, Franzson L, Jonsson JJ, Breen NN, Lesko BG, Berberich SL, Turner K, Ruoppolo M, Scolamiero E, Antonozzi I, Carducci C, Caruso U,Cassanello M, la Marca G, Pasquini E, Di Gangi IM, Giordano G, Camilot M, Teofoli F, Manos SM, Peterson CK, Mayfield Gibson SK, Sevier DW, Lee SY, Park HD, Khneisser I, Browning P, Gulamali-Majid F, Watson MS, Eaton RB, Sahai I, Ruiz C, Torres R, Seeterlin MA, Stanley EL, Hietala A, McCann M, Campbell C, Hopkins PV, de Sain-Van der Velden MG, Elvers B, Morrissey MA, Sunny S,Knoll D, Webster D, Frazier DM, McClure JD, Sesser DE, Willis SA, Rocha H, Vilarinho L, John C, Lim J, Caldwell SG, Tomashitis K, Castiñeiras Ramos DE, Cocho de Juan JA, Rueda Fernández I,Yahyaoui Macías R, Egea-Mellado JM, González-Gallego I, Delgado Pecellin C, García-Valdecasas Bermejo MS, Chien YH, Hwu WL, Childs T, McKeever CD, Tanyalcin T, Abdulrahman M, Queijo C,Lemes A, Davis T, Hoffman W, Baker M, Hoffman GL.
PMID:22766634[PubMed - in process]

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