Thermal activation of hexosaminidase A in a genetic compound with Tay‐Sachs disease

Ben‐Yoseph, Yoav; Baylerian, Michael S.; Momoi, Toru; Nadler, Henry L.

doi:10.1007/bf01800733

Cited by 8 publications

(4 citation statements)

References 13 publications

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“…Full-term placentae were collected at the time of delivery and kept frozen at -70 °C until used. Cultured skin fibroblasts from apparently normal individuals were obtained and maintained as previously described (Ben-Yoseph et al, 1983). Tissue and cells were homogenized in 4 vol.…”

Section: Materials and Methods Preparation Of Golgi Membranesmentioning

confidence: 99%

Molecular size of N-acetylglucosaminylphosphotransferase and α-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation

Ben‐Yoseph¹,

Potier²,

Pack³

et al. 1986

Biochemical Journal

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The radiation inactivation method was used to determine the molecular size of the two enzymes that participate in the synthesis of the phosphomannosyl recognition marker of lysosomal proteins. The determinations were carried out in situ, in Golgi membranes isolated from normal human placenta and cultured skin fibroblasts. A molecular size of 228 +/- 29 kDa was found for placental N-acetylglucosaminyl-phosphotransferase, and 129 +/- 11 kDa for placental alpha-N-acetylglucosaminyl phosphodiesterase. The values for the fibroblast enzymes were about 20% higher, 283 +/- 27 kDa and 156 +/- 14 kDa for the transferase and phosphodiesterase respectively. Triton X-100 had no effect on the molecular size of these enzymes.

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Section: Materials and Methods Preparation Of Golgi Membranesmentioning

confidence: 99%

Molecular size of N-acetylglucosaminylphosphotransferase and α-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation

Ben‐Yoseph¹,

Potier²,

Pack³

et al. 1986

Biochemical Journal

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“…Cultured skin fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy, and from apparently normal subjects, were obtained, maintained and harvested as previously described (Ben-Yoseph et al, 1983). Cell lines with the prefix GM were obtained from the NIGMS Human Genetic Mutant Cell Repository (Camden, NJ, U.S.A.).…”

Section: Cell Linesmentioning

confidence: 99%

Altered molecular size of N-acetylglucosamine 1-phosphotransferase in I-cell disease and pseudo-Hurler polydystrophy

Ben‐Yoseph

Potier

Mitchell

et al. 1987

Biochemical Journal

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The size of the mutant N-acetylglucosamine 1-phosphotransferase in Golgi membranes from fibroblasts of patients with I-cell disease and classical pseudo-Hurler polydystrophy, which comprised one complementation group characterized by deficiency towards both artificial and natural acceptor substrates, was significantly smaller than the normal enzyme, 151-174 kDa compared with 225-278 kDa. The size of the mutant enzyme from cell lines of patients with variant forms of pseudo-Hurler polydystrophy, which comprised another complementation group characterized by normal activity towards mono- and oligo-saccharide substrates, was significantly larger than the normal enzyme, ranging from 321 to 356 kDa in two families and from 528 to 547 kDa in a third family. These findings suggest that the mutations in I-cell disease and classical pseudo-Hurler polydystrophy result in a missing enzyme component, which renders the enzyme catalytically inefficient toward any type of acceptor substrate. In contrast, the mutations in the variant forms of pseudo-Hurler polydystrophy produce a larger enzyme molecule which is active toward small substrates but is incapable of binding natural lysosomal glycoprotein substrates.

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“…Cultured skin fibroblasts from patients with mu colipidosis IV and from apparently normal subjects were maintained and harvested as previously de scribed [22]. The mucolipidosis IV cell lines, GM02048, GM02527 and GM02528, were obtained from the NIGMS Human Genetic Mutant Cell Re pository (Camden, N.J., USA).…”

Section: Cell Linesmentioning

confidence: 99%

Stimulation of G(M3) Ganglioside Sialidase Activity by an Activator Protein in Patients with Mucolipidosis IV and Controls

Ben‐Yoseph

Mitchell

Yager

et al. 1991

Enzyme

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An activator protein that stimulates the enzymic hydrolysis of sialic acid from gangliosides by ganglioside sialidase was fractionated from human liver. This fraction was distinct from those stimulating the hydrolysis of galactose from G(M1) ganglioside by β-galactosidase and the hydrolysis of N-acetylgalactosamine from G(M2) ganglioside by hexosaminidase A. This fraction was highly specific for the hydrolysis of sialic acid from G(M3) ganglioside, and was equally effective in fibroblasts from patients with mucolipidosis IV and in fibroblasts from controls.

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Thermal activation of hexosaminidase A in a genetic compound with Tay‐Sachs disease

Cited by 8 publications

References 13 publications

Molecular size of N-acetylglucosaminylphosphotransferase and α-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation

Molecular size of N-acetylglucosaminylphosphotransferase and α-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation

Altered molecular size of N-acetylglucosamine 1-phosphotransferase in I-cell disease and pseudo-Hurler polydystrophy

Stimulation of G(M3) Ganglioside Sialidase Activity by an Activator Protein in Patients with Mucolipidosis IV and Controls

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