Journal of Protein Chemistry

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Complete amino acid sequence of jack bean urease
Journal of Protein Chemistry - Tập 6 - Trang 55-59 - 1987
Gunji Mamiya, Kunio Takishima, Mayumi Masakuni, Tatsuko Kayumi, Kazuko Ogawa
The subunit structure of jack bean urease has been unresolved in spite of many investigations. Thus far, the molecular weight for the native urease seem to range from 480,000 to 590,000 and the values for the monomer range from 30,000 to 97,000. The complete amino acid sequence of jack bean urease has been determined primarily by sequencing cyanogen bromide peptides, which were aligned by overlapp...... hiện toàn bộ
A Partially Unfolded State of Equine β-Lactoglobulin at pH 8.7
Journal of Protein Chemistry - Tập 20 - Trang 131-137 - 2001
Kazuo Fujiwara, Masamichi Ikeguchi, Shintaro Sugai
The urea-induced unfolding transition of equine β-lactoglobulin was studied at pH 8.7 using circular dichroism (CD), ultracentrifugation, and gel filtration chromatography. The unfolding transition curves showed that at least one intermediate accumulates at moderate concentrations of urea. Furthermore, analytical ultracentrifugation experiments indicated that the intermediate forms a dimer. Thus, ...... hiện toàn bộ
A Monomeric Mannose-Binding Lectin from Inner Shoots of the Edible Chive (Allium tuberosum)
Journal of Protein Chemistry - Tập 20 - Trang 361-366 - 2001
Y. W. Lam, T. B. Ng
A mannose-binding lectin was isolated from the inner shoots of the chive Allium tuberosum. The procedure involved aqueous extraction, (NH4)2SO4 precipitation, dialysis to remove (NH4)2SO4, affinity chromatography on mannose-agarose, ion exchange chromatography on SP-Sepharose, gel filtration on Superdex 75, and ion exchange chromatography on Mono S. Lectin activity was adsorbed on mannose-agarose,...... hiện toàn bộ
Kinetics of Thermal Inactivation of Lactate Dehydrogenase from Rabbit Muscle
Journal of Protein Chemistry - Tập 16 Số 8 - Trang 801-807 - 1997
Bai, Ji-Hong, Wang, Hao-Jing, Liu, De-Shan, Zhou, Hai-Meng
The kinetics of thermal inactivation of rabbit muscle lactate dehydrogenase at different temperatures has been studied using the kinetic method for the substrate reaction during irreversible inhibition of enzyme activity previously described by Tsou [Adv. Enzymol. Relat. Areas Mol. Biol. (1988), 61, 381–436]. The results show that thermal inactivation of the enzyme is an irreversible reaction. Mic...... hiện toàn bộ
The disulfide folding pathway of hirudin: A thrombin-specific inhibitor
Journal of Protein Chemistry - Tập 11 - Trang 416-417 - 1992
Jui-Yoa Chang, Benoit Chatrenet
Trapping succinimides in aged polypeptides by chemical reduction
Journal of Protein Chemistry - Tập 13 - Trang 89-96 - 1994
Darrick A. Carter, Philip N. McFadden
Cyclization of aspartic acid and asparagine to succinimides is thought to be a common spontaneous aging reaction in proteins, but the instability of the succinimide ring has made it difficult to directly measure this structure. Chemical reduction has now been tested as a means of trapping succinimides as stable derivatives, homoserine and isohomoserine. Two succinimide-containing compounds were te...... hiện toàn bộ
Affinity labeling of the active site of pig liver NADH-cytochrome b5 reductase by 5′-p-fluorosulfonylbenzoyladenosine
Journal of Protein Chemistry - Tập 5 - Trang 133-145 - 1986
Shiuan Chen, Mitsuru Haniu, Takashi Iyanagi, John E. Shively
Lysosome-solubilized pig liver NADH-cytochrome b5 reductase is inactivated by 5′-p-fluorosulfonylbenzoyladenosine (5′-FSBA) following pseudo-first-order kinetics. A double reciprocal plot of 1/Kobs versus 1/[5′-FSBA] yields a straight line with a positiveY intercept, indicative of reversible binding of the analogue prior to an irreversible incorporation.Kdor the initial reversible enzyme-analogue ...... hiện toàn bộ
Probing the Roles of the Only Universally Conserved Leucine Residue (Leu122) in the Oligomerization and Chaperone-like Activity of Mycobacterium tuberculosis Small Heat Shock Protein Hsp16.3
Journal of Protein Chemistry - - 2000
Hongzheng Dai, Qilong Mao, Wenxian Yang, Sufang Huang, Zengyi Chang
Erratum: Study of the Redox Properties of Metallothionein In Vitro by Reacting with DsbA Protein
Journal of Protein Chemistry - Tập 18 Số 8 - Trang 905-905 - 1999
H. Y. Hu, Haoyi Cheng, Q. Li, Yangbo Zhou, G. J. Xu
Assignment of the Disulfide Bridges in Bothropstoxin-I, a Myonecrotic Lys49 PLA2 Homolog from Bothrops jararacussu Snake Venom
Journal of Protein Chemistry - Tập 20 - Trang 377-382 - 2001
Adélia C. O. Cintra, Suely V. Sampaio, Arni K. Raghuvir, José R. Giglio
Bothropstoxin-I (BthTX-I), a Lys49 phospholipase A2 homolog with no apparent catalytic activity, was first isolated from Bothrops jararacussu snake venom and completely sequenced in this laboratory. It is a 121-amino-acid single polypeptide chain, highly myonecrotic, despite its inability to catalyze hydrolysis of egg yolk phospholipids, and has 14 half-cystine residues identified at positions 27,...... hiện toàn bộ
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