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'Peptide' in keywords Facet section ZfN Section C [X]

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1	Author	Dorothee Petz, Friedhelm Schneider	Requires cookie*
	Title	Kinetic Analysis of the Catalytic Properties of Peptides in Ester Hydrolysis
	Abstract	The catalytic properties of peptides containing histidine, cysteine and aspartic acid in ester hydrolysis were studied. Saturation kinetics were found for the reaction of p-nitrophenyl acetate (NPA) with Z-His-Ala-Asp-Gly-Cys-NH2 and Z-His-Ala-Gly-Gly-Cys-NH2 . The Brönsted equation for the hydrolysis of Zer«-butyloxycarbonyl-L-alanine-p-nitrophenylester (Boc-Ala-ONp) catalyzed by simple imidazole and SH-compounds was determined. The catalytic behaviour of the peptides in ester hydrolysis could not be described by the Brönsted equations for imidazole or thiole catalyzed hydrolysis of NPA and Boc-Ala-ONp. The pH dependence of the rate constants of the catalyzed ester hydrolysis gave no linear plots in 1 Jk versus H+ diagrams.
	Reference	(Z. Naturforsch. 31c, 675 [1976]; received September 20 1976)
	Published	1976
	Keywords	Kinetic Properties, Peptides, Ester Hydrolysis
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	TEI-XML for	default:Reihe_C/31/ZNC-1976-31c-0675.pdf
	Identifier	ZNC-1976-31c-0675
	Volume	31

2	Author	Amelia Thereza, Roberto Soares3, Ricardo Dias Lins3, RichardG. Longo3, Ricardo Arrattb, Ferreira3	Requires cookie*
	Title	Plural Origins of Molecular Homochirality in Our Biota Part II. The Relative Stabilities of Homochiral and Mixed Oligoribotides and Peptides
	Abstract	By computer simulations -molecular mechanics and molecular dynamics with the amber force field (Weiner et al., (1986), J. Comp. Chem. 7, 2 3 0 -2 5 2) -we have determined the stabilities of oligoribotide strands built with d -and L-riboses, and of peptide chains with d -and L-amino acid residues. In particular, complementary double-chains of oligoribotides were studied, since they are an important feature of the growing mechanism o f modern nucleic acids. Peptide chains on the other hand, grow without need of a template. We found that mixed oligoribotides are less stable than homochiral ones, and that this chiral effect is less noticeable in peptide chains. The results support the interpretation that L-riboses act as termi nators to the template-assisted growth of oligo-r-GD (enantiomeric cross-inhibition; Joyce et al., (1987), Proc. Natl. Acad. Sei. U S A 84, 4 398-4402). Based on this effect, a chemical pathway is proposed which could, under assumed prebiotic conditions, bypass the hindrance of homochiral growth.
	Reference	Z. Naturforsch. 52c, 89 (1997); received July 10/September 4 1996
	Published	1997
	Keywords	Chirality, Peptides, Oligoribotides, Computer Simulations
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	TEI-XML for	default:Reihe_C/52/ZNC-1997-52c-0089.pdf
	Identifier	ZNC-1997-52c-0089
	Volume	52

3	Author	Luigi Sportelli, H. Arald Neubacher, Wolfgang Lohmann	Requires cookie*
	Title	N O T I Z E N On the Influence of Arom atic R esidues on the Interaction of Copper (II) w ith Small P eptides Containing Arom atic Am ino Acids: ESR and Optical Studies
	Abstract	The complexation behaviour of C u(II) with di-and tri peptides containing the aromatic amino acids phenylalanine or tryptophan has been investigated at different pH-values and compared with results obtained with di-and triglycine. The results obtained by means of ESR and optical absorp tion spectroscopy show an influence of the two different aromatic entities on the magnetic and optical param eters. A significant decrease of the < 7\|\|-value and, concom ittantly, an increase of the energy of the d-d transition was m easured when an aromatic entity is present in the peptide. A possible explanation for this observation is given.
	Reference	(Z. Naturforsch. 32c, 643 [1977]; received May 4 1977)
	Published	1977
	Keywords	Copper (II)-Complexes, Peptides, Aromatic Amino Acids, Optical Absorption
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	TEI-XML for	default:Reihe_C/32/ZNC-1977-32c-0643_n.pdf
	Identifier	ZNC-1977-32c-0643_n
	Volume	32

4	Author	Karl Folkers, Cyril Bowers, Pui-FunL. Tang, Minoru Kobota, Xiao Shao-Bo, Wolf Gang Bender, Liu Yin-Zeng	Requires cookie*
	Title	Relative Potencies of Antagonists of the Luteinizing Hormone Releasing Hormone with Lys8 and Arg8 and Substitutions in Positions 3 ,5 ,6 ,7 and 8d-Ala10] — N H 2 and [N -A c—D-2
	Abstract	Antagonists of the luteinizing hormone releasing hormone (L H R H) of increased potency is a goal for control of ovulation. In the design and synthesis of 26 decapeptides, emphasis was given to analogs with Lys8 and Arg8 and with various substitutions in positions 3, 5, 6, 7 and 8. Two antagonists, [N — A c—D-2-Nal]-N H 2 showed 80-85% antiovulatory activity (A O A) at 0.25 (ig in the rat. The latter antagonist showed 60% A O A at 0.125 ^.g. O f four pairs of analogs with Arg8 and Lys8, respectively, two pairs favored Lys8 over Arg8 for potency. One pair showed negligible difference and another pair favored Arg8 over Lys8. There is specificity of substitution for potency. In other antagonists, d -3-Pal3, Tyr5 or Phe5, D-Arg6 and Leu7 or Nie7 or Val7 and Arg8 were variously effective substitutions for increase of potency and reduction of histamine release.
	Reference	Z. Naturforsch. 41c, 1087—1091 (1986); received June 10 1986
	Published	1986
	Keywords	Luteinizing Hormone Releasing Hormone, Ovulation, Peptide, Antagonist, Histamine Release
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	TEI-XML for	default:Reihe_C/41/ZNC-1986-41c-1087.pdf
	Identifier	ZNC-1986-41c-1087
	Volume	41

5	Author	Ernst Bayer, Heribert Hellstern, Heiner Eckstein	Requires cookie*
	Title	Synthese von immobilisierten Peptidfragmenten an Polystyrol-Polyoxyethylen zur Affinitätschromatographie Synthesis of Immobilized Peptide Fragments on Polystyrene-Polyoxyethylene for Affinity Chromatography
	Abstract	Polystyrene-polyoxyethylene craft copolymers have been used for step-wise peptide synthesis. After completion of synthesis the protecting groups are cleaved under acidic conditions, where the polymer-peptide bond is stable. These gels in comparison to polystyrene peptide gels, show better properties for applications in affinity chromatography as well as synthesis on solid supports, because the advantageous properties of polystyrene beads are combined with the excellent spacer behavior of polyoxyethylene chains (mobility, solvation by water and organic solvents). Peptide gels with polylysine sequences have been synthesized as highly selective stationary phases for the separation of the homologous oligo desoxyribonucleotides (d7)n with n = 1—3. The principal possibilities of these gels for affinity chromatography
	Reference	Z. Naturforsch. 42c, 455—460 (1987); received December 1 1986
	Published	1987
	Keywords	birthday Affinity Chromatography, Immobilization, Liquid-Solid-Phase, Peptides, Synthesis
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	TEI-XML for	default:Reihe_C/42/ZNC-1987-42c-0455.pdf
	Identifier	ZNC-1987-42c-0455
	Volume	42

6	Author	Toshiro Matsui, Tomoyuki Oki, Yutaka Osajima	Requires cookie*
	Title	Isolation and Identification of Peptidic a-Glucosidase Inhibitors Derived from Sardine Muscle Hydrolyzate
	Abstract	We report here the isolation of a-glucosidase (A G H) inhibitory peptides derived from sardine muscle hydrolyzate, which was prepared by digestion with Bacillus licheniformis alka line protease. A s a result of reversed-phase HPLC purification, two A G H inhibitory peptides were isolated from a D EA E -Sephadex A-25 column eluate. The peptides were identified as follows: V al-Trp (IC50 = 22.6 mM) and T ry -T y r -P r o -L e u (IC50 = 3.7 mM). A G H inhibitory studies of T r y -T y r -P r o -L e u and its derivatives demonstrated the importance of the tri peptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity.
	Reference	Z. Naturforsch. 54c, 259 (1999); received August 25/October 5 1998
	Published	1999
	Keywords	a-G lucosidase Inhibition, Diabetes, Sardine Muscle Hydrolyzate, Peptide
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	TEI-XML for	default:Reihe_C/54/ZNC-1999-54c-0259.pdf
	Identifier	ZNC-1999-54c-0259
	Volume	54

7	Author	H. Hauer, H.-D Lüdemann, R. Jaenicke	Requires cookie*
	Title	Free Activation Energies and Activation Volumes for the Amide Rotation in Some Peptides Studied by High Pressure 'H-High Resolution NMR
	Abstract	From the pressure dependence o f !H high resolution N M R spectra o f two dipeptides (glycylsarcosine and N-acetyl-L-proline-NH-methylamide in the range 0.1 MPa <.p< . 150 MPa the activation volumes A V* for the am ide rotation are derived. This conform ational transition is characterized for glycylsarcosine by A V* = 4 ± 1 cm3 • m ol-1 and for. the proline derivative by AV* = 1 .5 ± 1 cm3 • m ol-1. From the given results the m axim um contribution o f proline cis ^ trans isomerisation to the pressure dependence o f the rate o f reactivation of proteins can be estimated to ~ — 30% per M Pa and proline present.
	Reference	Z. Naturforsch. 37c, 51—56 (1982); received Septem ber 221981
	Published	1982
	Keywords	Activation Volume, High Pressure, NM R, Peptides, Proline-Isom erization
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	TEI-XML for	default:Reihe_C/37/ZNC-1982-37c-0051.pdf
	Identifier	ZNC-1982-37c-0051
	Volume	37

8	Author	H.Peter Matthiessen, H.Rainer Maurer	Requires cookie*
	Title	Low Molecular Mass Inhibitors from Calf Thymus Selective for T-Lymphocyte Proliferation
	Abstract	Endogenous factors preferentially inhibiting T-lympho-cyte proliferation were prepared from the acetone precipi tate of a 60% ethanol extract from calf thymus and their biochemical properties examined. By ultrafiltration the strongest lymphocyte-selective inhibition was found in the molecular mass range between 1 and 5 kDa. Fast protein liquid chromatography (FPLC) of this fraction on an anion exchange column eluted the lymphocyte inhibitors at 205—265 mM ammonium acetate. Staining procedures following IEF and TLC suggested, that the inhibitors may not be glycoconjugates or amines but small weakly acidic peptides (< 3 kDa).
	Reference	Z. Naturforsch. 41c, 1131 (1986); received November 11 1985/July 18 1986
	Published	1986
	Keywords	Lymphocyte Proliferation Inhibitors, Calf Thymus, Peptides, Chalone, Colony Formation
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	TEI-XML for	default:Reihe_C/41/ZNC-1986-41c-1131_n.pdf
	Identifier	ZNC-1986-41c-1131_n
	Volume	41

9	Author	IvankaG. Stankova3, M. Ario, F. Simeonovb, Vera Maximova0, AngelS. Galabov0, EvgenyV. Golovinskyd	Requires cookie*
	Title	Synthesis and Anti-Virus Activity of Some Nucleosides Analogues
	Abstract	New 3'-, 5'-, 5-bromo-2'-deoxyuridine (3 a -g) and 3'-, 5'-thymidine (4 a -i) analogues with amino acid and peptide residues were synthesized and evaluated for antiviral activity. The influence of long peptide chains, essential amino acids and the effect of this structural modifi cation on the antiviral activity has been also reported. Three 5-bromo-2'-deoxyuridine derivatives containing glycyl-, glycyl-glycyl-and glycyl-gly-cyl-glycyl-residues (3a, 3b, 3c) showed a strong activity against the herpes virus PsRV and a moderate one vs. HSV-1. The corresponding thymidine analogues were considerably less effective, and only com pounds 4d and 4h showed a borderline effect against PsRV.
	Reference	Z. Naturforsch. 54c, 75—83 (1999); received August lO/October 20 1998
	Published	1999
	Keywords	5-Bromo-2'-Deoxyuridine, Thymidine, Amino Acids, Peptides, Antiherpes Activity
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	TEI-XML for	default:Reihe_C/54/ZNC-1999-54c-0075.pdf
	Identifier	ZNC-1999-54c-0075
	Volume	54