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  • nuclear acetyltransferase  (2)
  • Cyclooxygenase  (1)
  • 1990-1994  (3)
  • 1
    Electronic Resource
    Electronic Resource
    High-mobility group and other nonhistone substrates for nuclear histoneN-acetyltransferase (1991)
    Springer
    Biochemical genetics 29 (1991), S. 461-475 
    Details
    ISSN: 1573-4927
    Keywords: nuclear acetyltransferase ; nonhistone substrate ; high-mobility group acetylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A variety of nonhistone proteins and polyamines has been studied for their substrate activity for nuclear histoneN-acetyltransferase. Nonhistone chromatin high-mobility group (HMG) proteins are found to be as good a substrate for the enzyme as histones. The enzyme also acetylates spermidine and spermine. However, protamine, bovine serum albumin, and ubiquitin are not substrates. Chymotryptic peptides of histone and HMGs retained about 64% of the substrate activity, but trypsin treatment reduced the substrate activity by more than 85%. BothN-acetyltransferase activities for HMGs and histones are copurified through salt extraction, polyethylene glycol fractionation, and chromatography on DEAE-cellulose, phosphocellulose columns, and a HPLC anionic-exchange column. The highly purified nuclear histone acetyltransferase shows similar optimalpH and ping-pong kinetics for both HMGs and histones. TheK m for HMG is 0.25 mg/ml. HMGs are able to accept the acetyl group from isolated acetyl-enzyme intermediate. Denatured gel analysis shows that HMG 1 and HMG 2 are the major proteins acetylated. High salt concentrations, mononucleotides, and DNA, which inhibit histone substrate activity of the enzyme, also inhibit HMG substrate activity. These observations suggest that there is a major nuclearN-acetyltransferase which is responsible for the acetylation of both histones and HMGs and perhaps also of spermine and spermidine. Thus the regulation of the structure and function of chromatin through postsynthetic acetylation can be achieved by a single nuclearN-acetyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554046
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  • 2
    Electronic Resource
    Electronic Resource
    High-mobility group and other nonhistone substrates for nuclear histoneN-acetyltransferase (1991)
    Springer
    Biochemical genetics 29 (1991), S. 461-475 
    Details
    ISSN: 1573-4927
    Keywords: nuclear acetyltransferase ; nonhistone substrate ; high-mobility group acetylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A variety of nonhistone proteins and polyamines has been studied for their substrate activity for nuclear histoneN-acetyltransferase. Nonhistone chromatin high-mobility group (HMG) proteins are found to be as good a substrate for the enzyme as histones. The enzyme also acetylates spermidine and spermine. However, protamine, bovine serum albumin, and ubiquitin are not substrates. Chymotryptic peptides of histone and HMGs retained about 64% of the substrate activity, but trypsin treatment reduced the substrate activity by more than 85%. BothN-acetyltransferase activities for HMGs and histones are copurified through salt extraction, polyethylene glycol fractionation, and chromatography on DEAE-cellulose, phosphocellulose columns, and a HPLC anionic-exchange column. The highly purified nuclear histone acetyltransferase shows similar optimalpH and ping-pong kinetics for both HMGs and histones. TheK m for HMG is 0.25 mg/ml. HMGs are able to accept the acetyl group from isolated acetyl-enzyme intermediate. Denatured gel analysis shows that HMG 1 and HMG 2 are the major proteins acetylated. High salt concentrations, mononucleotides, and DNA, which inhibit histone substrate activity of the enzyme, also inhibit HMG substrate activity. These observations suggest that there is a major nuclearN-acetyltransferase which is responsible for the acetylation of both histones and HMGs and perhaps also of spermine and spermidine. Thus the regulation of the structure and function of chromatin through postsynthetic acetylation can be achieved by a single nuclearN-acetyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02399688
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Biosynthesis of prostaglandins by human spermatozoa in vitro and their role in acrosome reaction and fertilization (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 33 (1992), S. 303-306 
    Details
    ISSN: 1040-452X
    Keywords: Arachidonic acid ; Calcium ionophores ; Cyclooxygenase ; Cyclooxygenase inhibitors ; Lipoxygenase products ; Phospholipase A2 ; Thromboxanes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Five homogenates of human sperm cells were separately incubated with [14C]arachidonic acid in the presence of reduced glutathione, L-tryptophan, and haematin as cofactors. The cyclooxygenase products of archidonic acid metabolism were extracted, separated, and measuréd for their radioactivity. The rate of formation of prostaglandin (PG)D2, PGE2, PGF2α, 6-keto PGF1α, and thromboxane (TX)B2 were 18.0 ± 1.11, 10.9 ± 0.68, 5.8 ± 0.21, 3.9 ± 0.13 and 6.6 ± 0.52 pmol/106 cells/min, respectively. These results are discussed in relation to the hypothesis that cyclooxygenase metabolites of certain polyunsaturated fatty acids play an important part in the sperm acrosome reaction and fertilization. © 1992 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080330311
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