GlycoWord / GlycogeneA-01 To understand the effects of the 1,4-galt-I deficiency on carbohydrate structures,N-glycans and O-glycans in various tissues of -1,4-galt-I KO mice were http://www.glycoforum.gr.jp/science/word/glycogene/GGA01.html
Extractions: -1,4-Galactosyltransferase ( -1,4-GalT) (EC 2.4.1.38) is a glycosyltransferase that is required for the biosynthesis of the backbone structure from type 2 chain (Gal 4GlcNAc), which appears widely on N-glcans, O-glycans and glycolipids. The type 2 chain is particularly important in the synthesis of sialyl lewis x and SSEA-1, which play a role in the immune system and early embryogenesis, respectively. Although -1,4-GalT gene was believed to be a single gene in the past, novel -1,4-GalT genes were successively isolated in 1997-1998 to form the -1,4-GalT gene family consisting of seven genes. KO mice deficient in the -1,4-GalT activity and faint bands corresponding to the Gal 4GlcNAc structure detected in -1,4-GalT-I KO mice could be derived from other -1,4-GalT gene(s). -1,4-GalT-I KO mice were unexpectedly born normally, although an essential role of the Gal -1,4-GalT-I KO mice showed augmented proliferation and abnormal differentiation of intestinal and epidermal epithelial cells, suggesting the carbohydratechains synthesized by -1,4-GalT-I regulate proliferation and differentiation of epithelial cells (1).
Requisition For Molecular Diagnostic Services FRAGILE X SYNDROME; FRIEDREICH S ATAXIA; GALACTOSEMIA (galactose1-phosphateuridyl transferase (galt) deficiency); HEMOCHROMATOSIS (HFE); HEMOGLOBIN C http://www.compgene.com/reqweb.htm
Extractions: Comprehensive Genetic Services SC, 3720 North 124th Street, Milwaukee, WI 53222 Toll free (877) COMPGENE or (414) 393 - 1000, FAX: (414) 393 - 1399 E-mail: compgene@worldnet.att.net DATE (MM/DD/YY): PATIENT NAME: DATE of BIRTH(MM/DD/YY): YOUR PATIENT ID# (if desired): REFERRING PHYSICIAN: ADDRESS TO SEND REPORT: ADDRESS TO SEND INVOICE: ETHNIC ORIGIN: SAMPLE TYPE: DATE SAMPLE OBTAINED(MM/DD/YY): INDICATION: FAMILY HISTORY? (Please FAX or enclose pedigree with samples)
Extractions: This Article Abstract Full Text (PDF) Alert me when this article is cited ... Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager ... Cited by other online articles PubMed PubMed Citation Articles by Scott, M. E. Articles by Koski, K. G. Journal of Nutrition.
Wisconsin Newborn Screening Laboratory: The genetic disturbance is expressed as a cellular deficiency of either Although detection of classical galactosemia using the galt enzyme test is not http://www.slh.wisc.edu/newborn/guide/galactosemia.php
Extractions: WSLH Newborn Guide Galactosemia ... Advisory Committee Health Professionals Guide to Newborn Screening: Newborn Screening Disorders Galactosemia Autosomal recessive disorder of galactose metabolism. The genetic disturbance is expressed as a cellular deficiency of either galactose-1-phosphate uridyl transferase (classic form), galactokinase, (variant) or uridine diphosphate galactose 4 epimerase (variant) - the enzymes catalyzing the reaction by which galactose is converted to glucose. The main dietary source of galactose is lactose, the principle carbohydrate in milk.
Galactose-1-phosphate Uridylyltransferase A deficiency of galt results in a clinical manifestation termed classicgalactosemia which may present a range of problems including neurological http://www.arches.uga.edu/~dan/bcmb8010/
Extractions: Please note these web pages are part of an assignment for a graduate course in Advanced Biochemistry and Molecular Biology BCMB8010 at the University of Georgia. Questions should be directed to Dan Sherling (dan@uga.edu) Structure of Galactose-1-phosphate uridylyltransferase (GALT) and its function in the Leloir Pathway The three steps of the Leloir pathway allows galactose (Gal), a metabolite of lactose, to enter the myrad of glucose (Glc) metabolic pathways by the conversion of Gal into UDP-glucose (UDP-Glc). In the first step, Gal is converted to galactose-1-phosphate (Gal1P) by galactokinase (GALK). Secondly, galactose-1-phosphate uridylyltransferase (GALT) catalyzes the transfer of one UMP from UDP-Glc to Gal1P, resulting in the production of Glc1P and UDP-galactose (UDP-Gal). UDP-Gal is then epimerized at the C4 position to produce UDP-Glc in the third (and final) step of the pathway by UDP-Gal epimerase (GALE). Glc1P may enter glycolysis through the conversion into Glc6P by phosphoglucomutase. In this report we will focus on the structure and function of the second enzyme in the Leloir pathway, GALT. GALT, a 379 amino acid homodimer in humans, catalyzes a double displacement reaction displaying ping-pong kinetics. First, UDP-Glc binds the enzyme through the nucleophilic attack of the enzymes His166 on the ?-phosphoryl of UDP-Glc. Glc1P is released, producing an uridylylated enzyme intermediate. The accepted mechanism shows GALT as being the only enzyme in the pathway that proceeds through a covalently bound intermediate. Secondly, Gal1P, from the GALK reaction, binds UMP at the enzymes active site, releasing UDP-Gal and regenerating the enzyme.
ACADM deficiency see mediumchain acyl-coenzyme A dehydrogenase deficiency Acid beta-glucosidase deficiency see Gaucher disease, type 1 http://www.urinator.com/testsavailable.htm
Extractions: A-T see ataxia-telangiectasia AAT see alpha-1 antitrypsin deficiency Absence of vas deferens see congenital bilateral absence of vas deferens Absent vasa see congenital bilateral absence of vas deferens ACADM deficiency see medium-chain acyl-coenzyme A dehydrogenase deficiency ACADVL see very long-chain acyl-coenzyme A dehydrogenase deficiency see achondrogenesis, type 1B see achondrogenesis, type 2 ACH see achondroplasia achondrogenesis, type 1B achondrogenesis, type 2 achondroplasia Acid beta-glucosidase deficiency see Gaucher disease, type 1 Acrocephalosyndactyly (Apert) see Apert syndrome acrocephalosyndactyly, type V see Pfeiffer syndrome Acrocephaly see Apert syndrome Acute cerebral Gaucher's disease see Gaucher disease, type 2 acute intermittent porphyria ACY2 deficiency see Canavan disease acyl-CoA dehydrogenase very long chain deficiency see very long-chain acyl-coenzyme A dehydrogenase deficiency AD see Alzheimer disease Adelaide-type craniosynostosis see Muenke syndrome Adenomatous Polyposis Coli see familial adenomatous polyposis Adenomatous Polyposis of the Colon see familial adenomatous polyposis ADP see ALAD deficiency porphyria Adrenal Gland Disorders see 21-hydroxylase deficiency Adrenogenital Syndrome see 21-hydroxylase deficiency AIP see acute intermittent porphyria AIS see androgen insensitivity syndrome AKU see alkaptonuria 5-ALA dehydratase-deficient porphyria see ALAD deficiency porphyria ALA-D porphyria see ALAD deficiency porphyria ALA dehydratase porphyria see ALAD deficiency porphyria ALAD deficiency porphyria Alagille syndrome Alcaptonuria
Chromatographia Online - July 54 Abstracts When applied to 11 anonymous blood spots of heterogeneous genotypes of GALTdeficiency all of the patients blood samples showed abnormal elevation of http://www.chromatographia.de/daten/july_54_abstracts.htm
Extractions: Volume (Issue): 54 July (1/2) 2001 Previous Issue Issue Listing Next Issue Some Studies of the Chromatographic Properties of Gels ('Artificial Antibodies/Receptors') for Selective Adsorption of Proteins D. Tong / Cs. Hetényi / Zs. Bikádi / J.-P. Gao / S. Hjertén non -charged monomers (acrylamide and N,N' Another universal method has been introduced for rapid screening of potential monomers and gels for the preparation of selective adsorbents. This very simple method is based on the assumption that the absorption maximum of a protein changes when the protein interacts with the free monomers or the adsorbent synthesized from the monomers (and does not change when the protein does not interact). Preliminary docking experiments indicate that selective adsorption of the protein by the polyacrylamide matrix is based primarily on hydrogen-bonding and dipole-dipole interactions. The strengths of these interactions can be varied by choosing different gel matrices (for removal of a given protein the interactions should be very strong, whereas they should be weaker for chromatographic analysis). Determination of the Antibiotic Zinc Bacitracin in Animal Food by High-Performance Liquid Chromatography with Ultraviolet Detection L. F. Capitán-Vallvey / N. Navas / A. Titos / R. Checa
