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  • 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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  • 3
    Electronic Resource
    Electronic Resource
    The conversion of ephedrine to methamphetamine and methamphetamine-like compounds during and prior to gas chromatographic/mass spectrometric analysis of CB and HFB derivatives (1992)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 21 (1992), S. 278-284 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Ephedrine and methamphetamine standards were separately derivatized with heptafluorobutyric anhydride (HFBA) and carbethoxyhexafluorobutyryl chloride (CB) and analyzed by full-scan gas chromatography/ion trap mass spectrometry with electron ionization (EI) and chemical ionization (CI). Using EI, a high-concentration ephedrine standard produced a total ion gas chromatogram containing several minor HFB derivatives in addition to ephedrine. One of these had the same retention time as the derivative of methamphetamine, while another eluted 3 s later. Both contained the same major mass fragmentation ions that could be erroneously used in targeted selected ion monitoring gas chromatographic/mass spectrometric analysis for methamphetamine. The full-scan EI and CI spectra showed that these derivatives were not methamphetamine. CI mass spectrometric studies of ephedrine scanning up to m/z 700 demonstrated that reaction with HFBA caused acylation of both the hydroxyl and secondary amino groups. The HFBA used in this study was contaminated with pentafluoropropionic anhydride and tri-fluoroacetic anhydride and produced mixtures of derivatives, some with retention times near or identical to that of methamphetamine. In contrast, CB derivatization of ephedrine produces a single methamphetamine-like compound that has the same retention time and mass spectra as methamphetamine, and is produced only when high gas chromatograph injector temperatures are used ( 〉 260°C). Collision-induced decomposition tandem mass spectrometric studies for the CB derivative verified that methamphetamine is produced from ephedrine at elevated GC injection port temperatures. In view of these findings, substance abuse testing for methamphetamine in urine must proceed with caution when ephedrine and other sympathomimetic amines are present. Definitive analyses can be accomplished by full-scan CI gas chromatographic/mass spectrometric analysis with HFB derivatives, or by lowering gas chromatograph injector temperatures with CB derivatives.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200210603
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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    A new technique for detecting oxytocinase activity in electrophoresis gels (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 396-397 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A sensitive staining method for the detection of oxytocinase (EC 3.4.11.3) activity in electrophoresis gels has been described. The method is based on the enzymatic release of p-nitroaniline (PNA) from two specific synthetic oxytocinase sub-strates, S-benzyl-L-cysteine-p-nitroanilide (BCN) and L-leucine-p-nitroanilide (LN), respectively. The PNA is then diazotized with sodium nitrite and subsequently coupled to a chromogen, N-(1-naphtyl)-ethylenediamine dihydrochloride (NED) to produce a deep pink/magenta colored azo-dye at the site of oxytocinase activity.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150130181
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  • 6
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    High-mobility group and other nonhistone substrates for nuclear histoneN-acetyltransferase (1991)
    Springer
    Details
    Publication Date: 1991-10-01
    Print ISSN: 0006-2928
    Electronic ISSN: 1573-4927
    Topics: Biology , Chemistry and Pharmacology
    Published by Springer
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  • 7
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    Crystal and molecular structures ofp-chlorophenyl-thiourea (I) and 2,4,6-tribromo-phenyl-thiourea (II) (1993)
    International Union of Crystallography
    Details
    Publication Date: 1993-08-21
    Print ISSN: 0108-7673
    Electronic ISSN: 2053-2733
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Published by International Union of Crystallography
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  • 8
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    Chemical crosslinking and the stabilization of proteins and enzymes (1992)
    Elsevier
    Details
    Publication Date: 1992-11-01
    Print ISSN: 0141-0229
    Electronic ISSN: 1879-0909
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Elsevier
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