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ENHANCEMENT Of ALPHA-CHYMOTRYPSIN-CATALYZED HYDROLYSIS Of SPECIfIC PARA-NITROANILIDE SUBSTRATES BY 4-PHENYLBUTYLAMINE DERIVATIVE Of HEN EGG-WHITE LYSOZYME

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BIOCHIMICA ET BIOPHYSICA ACTA 1978年第1期527卷 42-55页

作者： SHECHTER, Y GERTLER, A HEBREW UNIV JERUSALEM FAC AGR DEPT AGR BIOCHEM JERUSALEM 91000 ISRAEL WEIZMANN INST SCI DEPT ORGAN CHEM REHOVOT ISRAEL

Modification of hen egg-white lysozyme by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide in presence of 4-phenylbutylamine yielded derivatives, which contained 0.6-0.7 modified residues and retained about 60% of the original activity. Kinetic studies revealed that the modified-lysozyme increases approx. 20-fold the kcat of hydrolysis of SucGly2Phe-4-nitroanilide by .alpha.-chymotrypsin, without changing the Km. The apparent dissociation constant of phenylbutylamine-modified lysozyme .cntdot. chymotrypsin complex was 0.03 mM and independent of substrate concentration. The accelerating effect of the modified lysozyme was also observed with other p-nitroanilide substrates of .alpha.-chymotrypsin. The hydrolysis of other substrates, acylation by active site titrant or inhibition by irreversible or competitive inhibitors were unaffected. The enhancing effect of the modified lysozyme seems to be very specific since other chymotrypsin-like enzymes, or serine proteinases except .delta.-chymotrypsin, were not influenced and phenylbutylamine derivatives of .alpha.-lactalbumin or ribonuclease were lacking any enhancing effect. Smaller, but significant enhancing effect was found also in lysozyme substituted by benzylamine, .beta.-phenylethylamine and tryptamine and in inactive derivatives of lysozyme substituted by phenylbutylamine. Competitive inhibitors of lysozyme such as N-acetyl-D-glucose amine oligomers, (GlcNAc)2 and (GlcNAc)3 abolished partially the accelerating effect of phenylbutylamine-modified lysozyme, indicating that the substituted group is located in the vicinity of the binding site.

关键词： TosPheCk L-(1-tosylamido-2-phenyl)-ethyl chloromethyl ketone Ac N -acetyl Bz N -benzoyl Suc N -succinyl PhCH 2 SO 2 f phenylmethanesulfonyl fluoride, OME, methyl ester OEt ethyl ester

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LIMITED COOPERATIVITY IN COUPLING BETWEEN ELECTRON fLOW AND PHOTOSYNTHETIC ATP SYNTHESIS - COMPARATIVE-STUDY IN CHROMATOPHORES PHOSPHORYLATING AT VERY DIffERENT RATES

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fEBS LETTERS 1978年第2期87卷 323-328页

作者： CASADIO, R BACCARINIMELANDRI, A MELANDRI, BA UNIV BOLOGNA INST BOTI-40126 BOLOGNAITALY

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RECONSTITUTION Of ENERGY TRANSfORMER, GATE AND CHANNEL SUBUNIT REASSEMBLY, CRYSTALLINE ATPASE AND ATP SYNTHESIS

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BIOCHIMICA ET BIOPHYSICA ACTA 1978年第1期505卷 45-93页

作者： KAGAWA, Y Department of Biochemistry Jichi Medical School Minamikawachi Tochigi-ken 329-04 Japan

The concept of the pump, channel and gate used to explain transport, energy transforming systems and passage of an electric current through an excitable membrane is briefly described. Methods for isolating translocato... 详细信息

关键词： fCCP carbonylcyanide- p -trifluoromethoxyphenylhydrazone f 1 pump and gate portion of H + -ATPase, which shows ATPase activity f 0 , channel portion of H + -ATPase, which shows H + -channel activity H + -ATPase, proton-translocating adenosine riphosphatase Tricine, N -tris(hydroxy-methyl)methylglycine

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CRYSTAL-STRUCTURE ANALYSIS AND REfINEMENT Of 2 VARIANTS Of TRIGONAL TRYPSINOGEN - TRIGONAL TRYPSIN AND PEG (POLYETHYLENE-GLYCOL) TRYPSINOGEN AND THEIR COMPARISON WITH ORTHORHOMBIC TRYPSIN AND TRIGONAL TRYPSINOGEN

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fEBS LETTERS 1978年第2期90卷 265-269页

作者： BODE, W HUBER, R TECH UNIV MUNCHEN INST PHYS CHEMD-8033 MARTINSRIEDFED REP GER

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EVIDENCE fOR A NEW ELECTRON-DONOR TO P-700 IN CHLORELLA-PYRENOIDOSA

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fEBS LETTERS 1978年第1期94卷 100-104页

作者： BOUGESBOCQUET, B DELOSME, R Institut de Biologie Physico-Chimique 13 rue Pierre et Marie Curie 75005 Paris France

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GENERATION Of SUPEROXIDE ANION AS A SOURCE Of HYDROGEN-PEROXIDE IN A RECONSTITUTED MONO-OXYGENASE SYSTEM

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fEBS LETTERS 1978年第2期91卷 343-345页

作者： KUTHAN, H TSUJI, H GRAf, H ULLRICH, V WERRINGLOER, J ESTABROOK, RW UNIV SAARLAND DEPT PHYSIOL CHEMD-6650 HOMBURGFED REP GER UNIV TEXAS HLTH SCI CTRDEPT BIOCHEMDALLASTX 75235

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The efficiency of methionine incorporation from isoaccepting species of tRNA^Met into rabbit globin in an homologous reticulocyte lysate system

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BBA Section Nucleic Acids And Protein Synthesis 1978年第1期517卷 76-83页

作者： Richer, Leroy L. Department of Chemistry California Institute of Technology Pasadena CA United States

Rabbit globin α and β chains were labeled with [3H]leucine, and with [35S]methionine from reticulocyte tRNAMet isoacceptors using a rabbit reticulocyte cell-free synthesis system. [35S]Methionine from the three tRNA... 详细信息

Rabbit globin α and β chains were labeled with [³H]leucine, and with [³⁵S]methionine from reticulocyte tRNA^Met isoacceptors using a rabbit reticulocyte cell-free synthesis system. [³⁵S]Methionine from the three tRNA^Met species isolated by RPC-5 chromatography was incorporated into internal positions of both α and β globin. The initiator tRNA, tRNA^Met_I, exhibited very low efficiency for incorporating methionine internally, while tRNA^Met_II was four times more efficient than tRNA^Met_III. Amino acid analysis of the tryptic peptides of the labeled globins revealed that all three isoacceptors incorporated methionine into the normal methionine peptides. Similar studies with Escherichia coli [³⁵S]Met-tRNA^Met_f showed a 3-fold increase over the reticulocyte initiator tRNA in its capacity to incorporate methionine into the internal positions of rabbit globin. © 1978.

关键词： tRNA Met transfer RNA which can be aminoacylated with methionine in the presence of aminoacyl transfer RNA ligase (synthetase) Met-tRNA Met the aminoacylated form of tRNA Met tRNA Met f the methionine tRNA which recognizes the initiator codon and incorporates methionine predominantly at the N-terminal position RPC-5 reversed-phase chromatography as described by Kelmers and Heatherly [26]

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Studies on the mechanism of tris-induced inactivation of oxygen evolution

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BBA - Bioenergetics 1978年第2期502卷 321-344页

作者： Cheniae, G.M. Martin, I.f. Martin-Marietta Laboratories Baltimore MD United States

A study was made of the inactivation by Tris of O2 evolution in chloroplasts and the subsequent reactivation of O2 evolution. We conclude: 1. 1. At concentrations of Tris sufficient to inhibit O2 evolution directly, a... 详细信息

A study was made of the inactivation by Tris of O₂ evolution in chloroplasts and the subsequent reactivation of O₂ evolution. We conclude: 1. 1. At concentrations of Tris sufficient to inhibit O₂ evolution directly, a slow rate (t_{1 2} ≈ 20-25 min) of inactivation occurs;2. 2. Inactivation is accelerated (t_{1 2} ≈ 2 min) by weak light absorbed by system II and is rate limited by a dark step with a half-time of about 200 s;3. 3. Minimally one quantum event within System II is sufficient to inactive 50-70% of the O₂ evolving centers;4. 4. This process is 3-(3,4-dichlorophenyl)-1,1-dimethylurea insensitive but is inhibited by reduced dichlorophenol indophenol and phenazine methosulfate, carbonylcyanide-p-trifluoromethoxyphenylhydrazone, 2-(3-chloro-4-trifluoromethyl)-anilino-3,5-dinitrothiophene and tetraphenylboron;5. 5. Partial reactivation of inactive O₂ evolving centers is effected by the use of the same reagents inhibiting the light induced inactivations;6. 6. The life-time (t_{1 2} ≈ 1 to 3 h) of the activable state is correlated with diffusion across thylakoids of the larger manganese pool released from binding sites and remaining in thylakoids following inactivation of O₂ evolution. © 1978.

关键词： ANT-2p 2-(3-chloro-4-trifluoromethyl)-anilino-3,5-dinitrothiophene CCCP carbonylcyanide- m -chlorophenylhydrazone DCIP and DCIPH 2 oxidized and reduced forms of 2,6-dichlorophenol indophenol DCMU 3-(3,4-dichlorophenyl)-1,1-dimethylurea f and f ⨥ the precursor and the species yielding EPR Signal II fCCP carbonylcyanide- p -trifluoromethoxyphenylhydrazone f 0 the invariable fluorescence yield f max the maximum level of fluorescence Sig. II f and Sig. II vf the fast and very fast decaying species of EPR Signal II V quantum yield V max uncoupled rate at saturating intensity. Buffer 1, 0.4 M sucrose/0.05 M Tricine/0.02 M NaCl, pH 7.4

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Ultrastrukturanalyse der endoplasmatischen Algen von Amphistegina lessonii d'Orbigny, foraminifera (Protozoa) und ihre systematische Stellung)

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Archiv fur Protistenkunde 1978年第1-2期120卷 16-62页

作者： Berthold, Wulf-Ulrich Institut fü Biologie III Universität Tübingen Germany

The ultrastructure of the endoplasmic algae in adult (a. A.) and young Amphistegina lessonii (y. A.) is described, and compared with the situation in such algae, which show the same main chloroplast structures. The chloroplasts have lamellae without grana, the number of thylakoids per lamella is three, a girdle lamella is present. The chloroplasts are surrounded by a sheath of the endoplasmic reticulum which is continuous with the nuclear envelope. The pyrenoid (simple internal) is membrane bound in the algae of a. A. and not membrane bound in the algae of y. A. One or two thylakoids enter the pyrenoid. The golgi consists of two dictyosomes, associated to the nucleus. During mitosis a “spindle precursor” appears. The spindle is presumably formed extranuclear and sinks in the caryoplasm when the nuclear envelope breaks down. The spindle consists of one boundle of 19 microtubules. Centrioles are not present, but a “polar complex”. There exist oil droplets, vacuoles and a typical “vesicular complex”. Algae, living in the “Lakunen System” may have uncomplete skeleton like structures similar to a diatom frustule. They are not present in algae, lying in plasmatic vesicles of Amphistegina. The comparison with Phaeophyceae, Xanthophyceae, Chrysophyceae and Bacillariophyceae (Diatomeae) show, that the algae of Amphistegina are Diatoms. © 1978, All rights reserved.

关键词： A a. A. aC Alge Amphistegina, adult Amphistegina, juvenil C CH Chloroplast Chloroplastenhülle coated vesicles cV D db dense body Dictyosom eR eR endoplasmatisches Retikulum f GL Gürtellamelle H haustorienartiger Plasmastrang iC innere Calzitlage j. A. K Kernhülle Kernpore KH KP L La Lakunensystem Lamelle Lipidtropfen Lk M Mb Mi Microbodies Mitochondrium Mündung N Nukleolus ol organic lining organische Schicht oS P pc periplastidäre Zisterne PG PL Plasmalemma Plastoglobuli Po polar complex PoM Pore pore plug Porentrichter pp Primäre organische Membran Proloculus Ps Pseudopodien Pt Py Pyrenoid pZ R Residualkörper Ri Ribosom Silikalemma Sk Skelett SL Sp Spindel spindle precursor spp Stachel-Vesikel SV T Thylakoid V Vakuole Ve Vesikel Vesikel mit fibrillen vesikulärer Komplex vK W Wandung Z Zellkern Zentralkorn äuβere Calzitlage

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Two-step modification of aspartate aminotransferase with 1,5-difluoro-2,4-dinitrobenzene Cross-link localization

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BBA - Protein Structure 1978年第2期534卷 358-367页

作者： Deyev, S.M. Afanasenko, G.A. Polyanovsky, O.L. Institute of Molecular Biology Academy of Sciences the U.S.S.R. Moscow Russian Federation

At pH 7, the apoenzyme of carboxymethylated and acylated aspartate aminotransferase reacts selectively with 1,5-difluoro-2,4-dinitrobenzene to form a single intramolecular covalent bond with the ε{lunate}-amino group of the functional lysine residue located within the active centre. On shifting the pH to 9, the second fluorine atom of the bifunctional reagent is substituted with the sterically adjacent side groups of cysteine and tyrosine residues. The modified apoenzyme was subjected to partial proteolysis with pronase, and the digest was used to obtain and isolate the labeled products and to localize amino acid residues involved in the reaction. The established structures of several peptides containing Cys-2,4-dinitrobenzene-Lys and Tyr-2,4-dinitrobenzene-Lys allowed the identification of the amino acid residues involved in the reaction with the bifunctional reagent as Lys 258, Cys 390 and probably Tyr-70. The residues of Cys and Tyr are thus located at a distance of approximately 5 Å (the length of the dinitrophenylene bridge) from the lysine residue forming an aldimine bond with pyridoxal 5′-phosphate in the active site. © 1978.

关键词： f 2 N 2 ph, 1,5-difluoro-2,4-dinitrobenzene Cys-N 2 ph-Lys-1-( S -cysteil)-5-( N ϵ -lysyl)-2,4-dinitrobenzene Tyr-N 2 ph-Lys-1( O -tyrosyl)-5-( N ϵ -lysyl)-2,4-dinitrobenzene Bu-N 2 ph-Lys- S -butyl-5-( N ϵ -lysyl)-2,4-dinitrothiophenol

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