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| 2. |
- Chester, Alan, et al.
(författare)
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A new N-acetyl-beta-D-hexosaminidase disease with late onset of progressive neurological symptoms
- 1979
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Ingår i: Human Heredity. - 1423-0062. ; 29:2, s. 124-128
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Tidskriftsartikel (refereegranskat)abstract
- Clinical data are presented on a 30-year-old male with normal early development (4-5 years) but subsequent progressive impairment of psychomotor functions. He has marked kyphoscoliosis and talipes calcaneo-valgus. The organs appear normal and the patient can walk unaided and feed himself although he does not recognize his parents. He has normal fundi oculi. Biochemical data show an absence of mucopolysacchariduria and very low but detectable levels of N-acetyl-beta-D-hexosaminidase in serum and leucocytes. The clinical symptoms are much milder than would normally be expected from such a profound enzyme deficiency (Sandhoff disease).
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| 3. |
- Chester, Alan, et al.
(författare)
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The common identity of five glycosidases in human liver
- 1976
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Ingår i: Biochimica et Biophysica Acta. - 0006-3002. ; 429:2, s. 517-526
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Tidskriftsartikel (refereegranskat)abstract
- An enzyme has been isolated from human liver by DEAE-cellulose chromatography and has been shown by competitive substrate inhibition to be capable of hydrolysing synthetic beta-D-galactosides, beta-D-glucosides, beta-D-fucosides, beta-D-xylosides, and alpha-L-arabinosides. Another form of alpha-L-arabinosidase activity elutes with the major beta-D-galactosidase component on DEAE-chromatography, but has a different identity on the basis of its stability at 4 degrees C. Liver samples from patients with Gaucher's disease are deficient in beta-D-fucosidase as well as beta-D-glucosidase activity.
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| 4. |
- Chester, Alan, et al.
(författare)
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The relationship between different forms of human alpha-mannosidase
- 1975
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Ingår i: Biochimica et Biophysica Acta. - 0006-3002. ; 391:2, s. 341-348
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Tidskriftsartikel (refereegranskat)abstract
- The tissue distribution and some properties of human alpha-mannosidase (alpha-D-mannoside mannohydrolase EC 3.2.1.24) have been studied. The acidic forms of the enzyme were fairly stable, whereas the neutral forms easily lost enzymic activity. The acidic forms were sensitive to neuraminidase but the neutral forms were unaffected. The experiments indicate that the acidic components are closely related to each other, differing only in sialic acid content and possibly conformation. The neutral forms of the enzyme are probably quite different from the acidic forms both in structure and cellular function.
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