Synthetic Glycopeptide and Phosphopeptide Models of an Antibacterial Fragment of Chromogranin A. Pp. 143-150.
Mare Cudic, Philippe Bulet and
Laszlo Otvos, Jr.*
[Abstract]
Synthesis of Alzheimer’s b-Amyloid Peptide Fragment (33-42) on A New Chemically Inert Ps-Bdodma Support. Pp. 151-158.
M. Roice, K.S. Kumar*
& V.N. Rajasekharan Pillai
[Abstract]
An Apolipoprotein E Synthetic Peptide Targetslipid Particles to Lipoprotein Recptors. Pp. 159-166.
P.G. Lokhov*, O.M. Ipatova,
O.Yu. Abakumova, T.A. Prozorovskii
[Abstract]
3d-Structure of Human Seminal Plasma Prostatic Inhibin by Nonparametric Regression. Pp. 167-174.
Jyothi S. and Rajani R. Joshi*
[Abstract]
Single Chain Anti-Idiotypic Antibody Mimics of the Phytotoxin Dothistromin. Pp. 175-182.
Vadim L. Mett, William T.
Jones*, Valentina A. Mett, Dawn Harvey and Paul H.S. Reynolds
[Abstract]
Temperature Dependent Michaelis-Menten Analysis of The Bovine Adenosine Deaminase Catalyzed Deamination of Adenosine. Pp. 183-186.
Christian Castro and B. Mark
Britt*
[Abstract]
Predication of Some Spatial Structures of Proinsulin by Hydropathic Mass. Pp. 187-190.
Rong-Qiao HE* Yang
Liu, Ying Liu
[Abstract]
S-(1,2-Dicarboxyethyl)Glutathione Esters Elevate Glutathione Level in Human Hepatoma Hepg2 Cell. Pp. 191-195.
Seiji Tsuboi*,
Makoto Yasuda, and Satoshi Matsushima
[Abstract]
Crystalization and Preliminary X-Ray Analysis of Thermoactinomyces Vulgaris R-47 a-Amylase 1. Pp. 197-200.
Shin Kondo,
Akira Kaji1, Kazuyuki Yuguchi, Takashi Tonozuka, Yoshiyuki Sakano and Shigehiro
Kamitori*
[Abstract]
Crystalization and Preliminary X-Ray Analysis of Porcine Aldehyde Reductase in Complex with Coenzyme and Quercetin. Pp. 201-206.
Ossama
El-Kabbani* and Roland P.T.Chung
[Abstract]
[Back to top] Synthetic
Glycopeptide and Phosphopeptide Models of an Antibacterial Fragment of
Chromogranin A.
Mare Cudic, Philippe Bulet and Laszlo Otvos, Jr.
In order to fully characterize the activity spectrum and additional biochemical properties of native antimicrobial peptides corresponding to chromogranin A, we synthesized glycosylated, phosphorylated and double modified versions of the reportedly antibacterial 173-194 fragment. While no conformational change was detected, the modifications stabilized the peptide from proteolytic cleavage. All peptides remained inactive against a number of Gram-positive bacterial strains in the experimjental conditions used.
[Back to top] Synthesis of Alzheimer’s b-Amyloid Peptide Fragment (33-42) on A New
Chemically Inert Ps-Bdodma Support.
M. Roice, K.S. Kumar* & V.N. Rajasekharan Pillai
The (33-42) fragment of Alzheimer’s b-amyloid peptide (Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala) was synthesized on a 2% 1,4-butanediol dimethacrylate cross-linked polystyrene (PS-BDODMA) support. The new polymer support was prepared by aqueous free-radical suspension polymerization of styrene and 1,4-butanediol dimethacrylate. The peptide was synthesized using Boc-amino acids and cleaved from the resin by trifluoroacetic acid (TFA) in high purity and yield. The Crude peptide was purified by HPLC and characterized by amino acid analysis and MALDI TOF MS.
[Back to top] An Apolipoprotein E Synthetic Peptide Targetslipid
Particles to Lipoprotein Recptors.
P.G. Lokhov*, O.M. Ipatova, O.Yu. Abakumova, T.A. Prozorovskii
An apolipoprotein E 139-158 synthetic peptide was tested for targeting lipid particles to lipoprotein receptors. In was shown that this peptide increases lipid particle binding followed by receptor-mediated endocytosis by cells. In addition, the peptide mediates both acute clearance of lipoproteins followed by the decrease of cholesterol level in a rat blood and acute uptake of liposomes by the tissues which have a high level expression of lipoprotein receptors.
[Back to top] 3d-Structure of Human Seminal Plasma Prostatic
Inhibin by Nonparametric Regression.
Jyothi S. and Rajani R. Joshi*
Human Seminal Plasma Prostatic Inhibin (HSPI) is a biologically important protein of 94 amino acids isolated from the human prostate glands. No. information is yet available on its 3d-structure. Here, we use a nonparametric regression approach to determine the 3d-structure of HSPI. This approach has been validated earlier and is found to be better in accuracy and efficiency than other computational approaches. The structure predicted by us agrees with the properties of HSPI deciphered experimentally.
[Back to top] Single Chain Anti-Idiotypic Antibody Mimics of the
Phytotoxin Dothistromin.
Vadim L. Mett, William T. Jones*, Valentina A. Mett, Dawn Harvey and Paul H.S. Reynolds
A single chain antibody mimic (MScFv10E7) was constructed, using a phage display recombinant antibody system, from RNA isolated from the splenocytes of mice immunized with monoclonal antibody Mab10C12 which recognizes the furan ring of DOTH [1]. MScFV10E7 competed with DOTH for binding to Mab10C12 in two ELISA formats and also reacted with the DOTH binding protein [2] extracted from mature Pinus radiata embryos and is a b-type anti-idiotypic mimic of DOTH.
[Back to top] Temperature Dependent Michaelis-Menten Analysis of
The Bovine Adenosine Deaminase Catalyzed Deamination of Adenosine.
Christian Castro and B. Mark Britt*
Michaelis-Menten analysis of the bovine adenosine deaminase catalyzed deamination of adenosine from 10.0-40.0oC and at its pH optimum (pH=6.3) is reported. It is found that KM increases gradually and nearly linearly with T and exhibits a minimum between 10 and 15oC. The relative increase of kcat with T is more pronounced and very linear. Values at the physiologic T of 38.3oC are: KM = 26+2 mM; kcat = 99+4 s-1. The pseudosecond order rate constant (kcat/KM) has a maximal value of ~3.8 mM-1S-1 in the physiological temperature range.
[Back to top] Predication of Some Spatial Structures of Proinsulin
by Hydropathic Mass.
Rong-Qiao HE* Yang Liu, Ying Liu
Hydropathic mass (HM) has been used to display the characterization of hydrophilicity and hydrophobicity of proinsulin. The a-helix of the B chain (residues 9-19), which is located at the inner part of the crystalline insulin, possesses a strong positive HM. The proteolytic sites of proinsulin for insulin maturation are located in the most negative HM regions. This suggests that they are exposed to the exterior of the molecule, which contributes to the digestion by proteases during insulin maturing.
[Back to top] S-(1,2-Dicarboxyethyl)Glutathione Esters Elevate
Glutathione Level in Human Hepatoma Hepg2 Cell.
Seiji Tsuboi*, Makoto Yasuda, and Satoshi Matsushima
The elevating effect of S(1,2-dicarboxyethyl) glutathione (DCE-GS) esters on the glutathione (GSH) content was examined using human hepatocellular carcinoma cell line HepG2. The treatment with DCE-GS diester and triester (0.5 mM). Increased the GSH level in HepG2 cells up to 145% over control level after 24h, respectively. DCE-GS diester and triester also elevated g-glutamylcysteine synthestase (g-GCS) activity in HepG2 cells up to 125 and 150% over the control level after 24h, respectively. However, this elevation of g-GCS did not occur on treatment with bis-(p-nitrophenyl)phosphate, non-specific esterase inhibitor. It is therefore concluded that DCE-GS diester and triester are transported into cells and hydrolyzed intracellularly to DCE-GS, and then DCE-GS produced promotes GSH synthesis due to the activation of g-GCS.
[Back to top] Crystalization and Preliminary X-Ray Analysis of Thermoactinomyces Vulgaris R-47 a-Amylase 1.
Shin Kondo, Akira Kaji1, Kazuyuki Yuguchi, Takashi Tonozuka, Yoshiyuki Sakano and Shigehiro Kamitori*.
Crystals of Thermoactinomyces vulgaris R-47 a-amylase 1, hydrolyzing cyclodextrins and pullulan, were grown by the vapor diffusion methods in two crystal forms with minor variations. The diffraction data were collected up to 2.5 Å resolution and both crystals were belong to monoclinic system and a space group of C2 with cell dimensions of a = 123.6 Å, b = 51.7 Å, and c = 109.1 Å, b = 104.2o (crystal form 1) and a = 122.5 Å, b = 55.0 Å, and c = 108.7 Å, b = 103.8o (crystal form 2).
[Back to top] Crystalization and Preliminary X-Ray Analysis of Porcine Aldehyde Reductase in Complex with Coenzyme and Quercetin.
Ossama
El-Kabbani* and Roland P.T.Chung
Aldehyde reductase, member of the aldo-keto reductase superfamily, catalyzes the reduction of a variety of aldehydes and ketones to their corresponding alcohols. Hexagonal cryustals of porcine aldehyde reductase in complex with NADPH and the flvonoid inhibitor quercetin have been grown using the hanging-drop vapour-diffusion method with ammonium sulfate as precipitant. The b9inding of quercetin into the active site of aldehyde reductase was rev3ealed from a difference electron density map. This is the first cystallization report of an aldo-keto reductase in complex with aflavonoid.