Detail of "2776-93-4"

Reference

Enzymic determination of urinary aspartylglucosylamine: a rapid and sensitive method to detect aspartylglucosylaminuria (AGU)

Enzymic determination of urinary aspartylglucosylamine: a rapid and sensitive method to detect aspartylglucosylaminuria (AGU). Sugahara, K.; Nishimura, K.; Aula, P.; Yamashina, I. (Fac. Pharm. 9075-24-5 and 2776-93-4 are also occured in this study. Sci., Kyoto Univ., Kyoto, Japan). Clin. Chim. Acta, 72(2), 265-7 (English) 1976. CODEN: CCATAR. DOCUMENT TYPE: Journal CA Section: 9 (Biochemical Methods) Section cross-reference(s): 14 An enzymic method that uses aspartylglucosylamine amidohydrolase (EC 3.5.1.26) (amidase) is described for screening urine samples specifically for aspartylglucosylamine (I) in the diagnosis of the title hereditary disease, AGU. Thus, to a 0.24-ml urine sample was added 2 milliunits hog kidney amidase in pH 5.5 buffer contg. enzyme stabilizers, and the mixt. was incubated for 22 h at 37.degree.. Na borate (pH 9.1) was added, and the mixt. was heated in boiling water for 9 min. After cooling and addn. of Ehrlich reagent, the color developed after 20 min at 37.degree. was detd. spectrometrically at 585 nm. The reaction depended crit. upon pH and heating time. AGU urines gave values of 0.193-0.295 mg I/l., which were distinct from values for the urine of heterozygotes (0-44) or normals (0-6). .

Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene

Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene. Mononen, Ilkka; Heisterkamp, Nora; Kaartinen, Vesa; Mononen, Tarja; Williams, Julian C.; Groffen, John (Div. Med. Genet., Child. Hosp. Los Angeles, Los Angeles, CA 90054-0700, USA). J. 9075-24-5 and 2776-93-4 are cas registry numbers. These chemicals are also mentioned in this article. Biol. Chem., 267(5), 3196-9 (English) 1992. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 14 (Mammalian Pathological Biochemistry) Section cross-reference(s): 3 Aspartylglycosaminuria is a lysosomal storage disease caused by deficient activity of glycoasparaginase (EC 3.5.1.26), and it occurs with a high frequency among Finns. The mol. defect in all Finnish aspartylglycosaminuria patients examd. to date consists of two single base changes in the heavy chain of glycoasparaginase. This is the first report on the identification of the mol. defect causing aspartylglycosaminuria in a patient of non-Finnish origin. Total RNA from fibroblasts of a black American aspartylglycosaminuria patient was isolated, first-strand cDNA was synthesized, and the cDNA encoding glycoasparaginase was amplified by the polymerase chain reaction. The patient's mRNA nucleotide sequence was different from the normal sequence by a deletion of 134 nucleotides at positions 807-940. Nucleotide sequence anal. of the normal glycosasparaginase gene demonstrated that the deletion corresponded precisely to a 134-base pair exon. Moreover, anal. of the splice sites demonstrated a single base change, G to T, that altered the donor splice site of the exon deleted in the patient's mRNA. This change led to an exon-skipping event resulting in a frame shift and generation of a stop codon. .