Journal of Protein Chemistry

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SDS-Induced Conformational Changes and Inactivation of the Bacterial Chaperonin GroEL
Journal of Protein Chemistry - Tập 18 - Trang 653-657 - 1999
Sen Li, Liao-Teng Wang, Hai-Meng Zhou
The inactivation and conformational changes of the bacterial chaperonin GroEL have been studied in SDS solutions with different concentrations. The results show that increasing the SDS concentration caused the intrinsic fluorescence emission intensity to increase and the emission peak to slightly blue-shift, indicating that increasing the SDS concentration can cause the hydrophobic surface to be s...... hiện toàn bộ
The hemolymph coagulation system in invertebrate animals
Journal of Protein Chemistry - - 1986
Sadaaki Iwanaga, Takashi Morita, Toshiyuki Miyata, Takanori Nakamura, Jun Aketagawa
A hemocyte lysate from horseshoe crab produced a gel, when exposed to Gram-negative bacterial endotoxins. This gelation reaction of the lysate, so-called Limulus test, has been widely employed as a simple and very sensitive assay method for endotoxins. Recent biochemical studies on the principle of Limulus test indicate that the hemocytes contain several serine protease zymogens, which constitute ...... hiện toàn bộ
Position of the sulfhydryl group and the disulfide bonds of human glucocerebrosidase
Journal of Protein Chemistry - Tập 14 - Trang 127-137 - 1995
Yonih Lee, Haruyuki Kinoshita, Gary Radke, Solly Weiler, John A. Barranger, John M. Tomich
Purified human glucocerebrosidase isolated from placenta was modified with [14C]-iodoacetic acid without reduction and digested with both protease-V8 at pH 4.0 followed byα-chymotrypsin at pH 7.5. The majority of radioactivity was found in a peptide that contained the [14C]-carboxymethylated-cysteine identified as CM-Cys18. Direct sequencing of the N-terminus of the intact labeled protein confirme...... hiện toàn bộ
G-proteins in neuronal and sensory tissue from invertebrates
Journal of Protein Chemistry - Tập 8 - Trang 374-375 - 1989
K. Raming, I. Boekhoff, J. Strotmann, H. Breer
A Catalytic Antibody That Accelerates the Hydrolysis of Carbonate Esters. Prediction of the Binding-Site Structure of the Substrate
Journal of Protein Chemistry - Tập 17 - Trang 273-278 - 1998
Haruo Suzuki, Etsuko B. Mukouyama, Chieki Wada, Yasuko Kawamura-Konishi, Yumiko Wada, Mitsunori Ono
Monoclonal antibodies catalyzing the hydrolysis of p-nitrophenyl alkyl carbonate were obtained using p-nitrophenyl phosphonate as hapten. One of the antibodies, 4A1, has a relatively high activity for the substrate having a bulky group. To determine the amino acid residues related to the binding of the bulky group, we determined the amino acid sequences of VL and VH regions of 4A1 by the cycle seq...... hiện toàn bộ
Expression of A Chain and B Chain of β-Bungarotoxin from Taiwan Banded Krait: The Functional Implication of the Interchain Disulfide Bond Between A Chain and B Chain
Journal of Protein Chemistry - Tập 20 - Trang 413-421 - 2001
Pei-Fung Wu, Long-Sen Chang
β-Bungarotoxin (β-Bgt), the main presynaptic neurotoxin purified from the venom of Bungarus multicinctus, consists of two dissimilar polypeptide chains, the A chain and B chain, cross-linked by an interchain disulfide bond. The A and B chain cDNAs were subcloned into expression vectors pT7-7 and pET20b(+), respectively, and transformed into Escherichia coli strain BL21(DE3). The expressed protein ...... hiện toàn bộ
Thermal Stability of Phosphoenolpyruvate Carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae
Journal of Protein Chemistry - Tập 22 - Trang 311-315 - 2003
M. Cristina Ravanal, Hughes Goldie, Emilio Cardemil
The quaternary structure of ATP-dependent phosphoenolpyruvate (PEP) carboxykinases is variable. Thus, the carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae are monomer, homodimer, and homotetramer, respectively. In this work, we studied the effect of temperature on the stability of the enzyme activity of these three carboxykinases, and have found that it follow...... hiện toàn bộ
The complete amino acid sequence of bovine antithrombin (ATIII)
Journal of Protein Chemistry - Tập 10 - Trang 205-212 - 1991
H. Mejdoub, M. Le Ret, Y. Boulanger, M. Maman, J. Choay, J. Reinbolt
Bovine antithrombin (ATIII) is a glycoprotein of Mr 56,600. Its primary structure was established using peptide sequences from five different digests. Bovine ATIII exhibits four glycosylation sites as well as human ATIII. The primary structures of bovine and human ATIII were compared: all the residues required for the integrity of the heparin-binding domain are strictly conserved. However, there a...... hiện toàn bộ
The selectivity filter of a ligand-gated ion channel
Journal of Protein Chemistry - Tập 8 - Trang 327-329 - 1989
Ferdinand Hucho, Rolf Hilgenfeld
Analysis of Aluminum—Yeast Hexokinase Interaction: Modifications on Protein Structure and Functionality
Journal of Protein Chemistry - - 2000
J. M. Socorro, R. Olmo, C. Teijón, M. D. Blanco, J. M. Teijón
The aluminum and yeast hexokinase interaction was studied. Structural changes were correlated with variations in protein functionality. Results show two different behaviors: At low metal concentrations preferential adsorption of metal (and water exclusion) induces aggregate formation. No significant changes in the protein structure occur, but there is a continuous loss of activity (from the first ...... hiện toàn bộ
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