Literature DB >> 3019310

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

Y Ben-Yoseph, M Potier, B A Pack, D A Mitchell, S B Melançon, H L Nadler.   

Abstract

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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Year:  1986        PMID： 3019310      PMCID： PMC1146769          DOI： 10.1042/bj2350883

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  20 in total

Review 1.  Size determination of enzymes by radiation inactivation.

Authors:  E S Kempner; W Schlegel
Journal:  Anal Biochem       Date:  1979-01-01       Impact factor: 3.365

2.  Membrane enzyme systems. Molecular size determinations by radiation inactivation.

Authors:  G R Kepner; R I Macey
Journal:  Biochim Biophys Acta       Date:  1968-09-17

3.  Enzymatic phosphorylation of lysosomal enzymes in the presence of UDP-N-acetylglucosamine. Absence of the activity in I-cell fibroblasts.

Authors:  A Hasilik; A Waheed; K von Figura
Journal:  Biochem Biophys Res Commun       Date:  1981-02-12       Impact factor: 3.575

4.  A method for rapid isolation of rough and smooth microsomes and Golgi apparatus from rat liver in the same sucrose gradient.

Authors:  P O Sandberg; L Marzella; H Glaumann
Journal:  Exp Cell Res       Date:  1980-12       Impact factor: 3.905

5.  Identification of a variant of mucolipidosis III (pseudo-Hurler polydystrophy): a catalytically active N-acetylglucosaminylphosphotransferase that fails to phosphorylate lysosomal enzymes.

Authors:  A P Varki; M L Reitman; S Kornfeld
Journal:  Proc Natl Acad Sci U S A       Date:  1981-12       Impact factor: 11.205

6.  Identification of a rat liver alpha-N-acetylglucosaminyl phosphodiesterase capable of removing "blocking" alpha-N-acetylglucosamine residues from phosphorylated high mannose oligosaccharides of lysosomal enzymes.

Authors:  A Varki; S Kornfeld
Journal:  J Biol Chem       Date:  1980-09-25       Impact factor: 5.157

7.  Radiometric assays of N-acetylglucosaminylphosphotransferase and alpha-N-acetylglucosaminyl phosphodiesterase with substrates labeled in the glucosamine moiety.

Authors:  Y Ben-Yoseph; M S Baylerian; H L Nadler
Journal:  Anal Biochem       Date:  1984-11-01       Impact factor: 3.365

8.  Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal alpha-N-acetylglucosaminyl phosphodiesterase.

Authors:  A Waheed; A Hasilik; K von Figura
Journal:  J Biol Chem       Date:  1981-06-10       Impact factor: 5.157

9.  Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity.

Authors:  M L Reitman; A Varki; S Kornfeld
Journal:  J Clin Invest       Date:  1981-05       Impact factor: 14.808

10.  Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes.

Authors:  M L Reitman; S Kornfeld
Journal:  J Biol Chem       Date:  1981-12-10       Impact factor: 5.157
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  2 in total

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

Authors:  Y Ben-Yoseph; M Potier; D A Mitchell; B A Pack; S B Melançon; H L Nadler
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

2.  Mucolipidoses II and III variants with normal N-acetylglucosamine 1-phosphotransferase activity toward alpha-methylmannoside are due to nonallelic mutations.

Authors:  Y Ben-Yoseph; D A Mitchell; R M Yager; J T Wei; T H Chen; L Y Shih
Journal:  Am J Hum Genet       Date:  1992-01       Impact factor: 11.025
  2 in total

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