Evidence for two variants of poly(adenosine diphosphate ribose) glycohydrolase in rat testis

Burzio, Luis O.; Riquelme, Patricio T.; Ohtsuka, Eiji; Koide, S. S.

doi:10.1016/0003-9861(76)90264-2

Cited by 39 publications

(13 citation statements)

References 34 publications

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“…Because the analysis of the purified enzyme preparation by non-denaturing gel electrophoresis was not successful, it is difficult to interpret the significance of the two bands. Howevcr, Burzio et al [27] report the existence of two variants or glycohydrolase in rat testis. Glycohydrolase exists in both tightly and loosely bound forms in nuclei.…”

Section: Discussionmentioning

confidence: 99%

“…The unadsorbed protein possessed about 25",, of thc total enzyme activity applied to the column. This may have been due to association of enzyme with nucleic acid [25,27].…”

Section: Pir R I F I'cnmentioning

confidence: 99%

“…It has also becn partially purified from P. polj~ceplzalurn [29], rat testis [27] and rat liver [23]. We have purified the poly(ADP-ribose) glycohydrolase from pig thymus 12300-fold and have determined some of the properties of the enzyme.…”

mentioning

confidence: 99%

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Isolation and purification of poly(ADP‐ribose) glycohydrolase from pig thymus

Tavassoli

Shall

1983

European Journal of Biochemistry

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Poly(ADP‐ribose) glycohydrolase has been purified about 12 300‐fold from pig thymus with a recovery of 8.5%. The specific activity of the purified enzyme is 13.8 μmol min−1 mg protein−1. The molecular weight was estimated to be 59000 by gel filtration through Sephadex G‐100 in a non‐denaturing solvent. Analysis of the final preparation by sodium dodecyl sulphate gel electrophoresis reveals two protein bands of molecular weigth, 61 500 and 67 500. The Km value for poly(ADP‐ribose) is estimated to be 1.8 μM monomer units. The enzyme preparation is free from phosphodiesterase, NADase and ADP‐ribosyltransferase activities. The purified enzyme is inhibited by cyclic AMP, ADP‐ribose, naphthylamine, histones H1, H2A, H2B, H3, polylysine, polyarginine, polyornithine and protamine. The inhibition by histone is relieved by an equal mass of DNA. Single‐stranded DNA, poly(A), poly(I) and polyvinyl sulphate were inhibitory, but double‐stranded DNA was not inhibitory.

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Section: Discussionmentioning

confidence: 99%

“…The unadsorbed protein possessed about 25",, of thc total enzyme activity applied to the column. This may have been due to association of enzyme with nucleic acid [25,27].…”

Section: Pir R I F I'cnmentioning

confidence: 99%

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Isolation and purification of poly(ADP‐ribose) glycohydrolase from pig thymus

Tavassoli

Shall

1983

European Journal of Biochemistry

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“…Poly(ADP-ribose)glycohydrolase was assayed as in [6] using poly(ADP-ribose) synthesized from isolated nuclei and purified as in [7]. RNA polymerase was assayed as in [4].…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…RNA polymerase was assayed as in [4]. The poly(ADPribose)polymerase products were analyzed as in [8] and the glycohydrolase products by the method in [6] except that cellulose polythyleneimine plates were used for the chromatograms. DNA was estimated by the Burton method [9] and protein by the Lowry method [IO].…”

Section: Enzyme Assaysmentioning

confidence: 99%