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LC-MS/MS method for the quantitation of serum tocilizumab in rheumatoid arthritis patients using rapid tryptic digestion without IgG purification

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Journal of Pharmaceutical Analysis 2022年第6期12卷 852-859页

作者： Takashi Mochizuki kaito shibata Takafumi Naito Kumiko Shimoyama Noriyoshi Ogawa Masato Maekawa Junichi Kawakami Department of Hospital Pharmacy Hamamatsu University School of MedicineHamamatsu431-3192Japan Department of Pharmacy Shinshu University HospitalMatsumotoNagano390-8621Japan Third Division Department of Internal MedicineHamamatsu University School of MedicineHamamatsu431-3192Japan Department of Laboratory Medicine Hamamatsu University School of MedicineHamamatsu431-3192Japan

The quantitation of serum tocilizumab using liquid chromatography tandem-mass spectrometry(LC-MS/MS)method has not been widely applied in clinical settings because of its time-consuming and costly sample *** present study aimed to develop a validated LC-MS/MS method for detecting serum tocilizumab by utilizing immobilized trypsin without an immunoglobulin G purification step and evaluate its applicability in the treatment of rheumatoid arthritis(RA)patients administered intravenously or subcutaneously with *** tocilizumab-derived signature peptide was deciphered using a nano-LC system coupled to a hybrid quadrupole-orbitrap mass *** serum tocilizumab was rapidly digested by immobilized trypsin for 30 *** chromatographic peak of the signature peptide and that of the internal standard were separated from the serum digests for a total run time of 15 *** calibration curve of serum tocilizumab concentration was linear with a range of 2-200 μg/*** intra-and inter-day accuracy and relative standard deviation(RSD)were 90.7%-109.4%and<10%,*** serum tocilizumab concentrations in the RA patients receiving intravenous and subcutaneous injections were 5.8-28.9 and 2.4-63.5 μg/mL,*** serum tocilizumab concentrations using the current method positively correlated with those using the enzyme-linked immunosorbent assay,although a systematic error was observed between these *** conclusion,a validated LC-MS/MS method with minimal sample pretreatments for monitoring serum tocilizumab concentrations in RA patients was developed.

关键词： Tocilizumab LC-MS/MS Immobilized trypsin IgG purification Proteomics Rheumatoid arthritis

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Effect of branched-chain amino acids in patients receiving intervention for hepatocellular carcinoma

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World Journal of Gastroenterology 2014年第10期20卷 2673-2680页

作者： Tomoaki Ishihara Motoh Iwasa Hideaki Tanaka Masahiko kaito Jiro Ikoma Toshiya shibata Yoshiyuki Takei Department of Gastroenterology and Hepatology Yokkaichi Digestive Disease Center Komono Mie 510-1232 Japan Department of Gastroenterology and Hepatology Mie University Graduate School of Medicine Tsu Mie 514-8507 Japan Department of Gastroenterology and Hepatology Mie Shokakinaika Tsu Mie 514-0062 Japan Department of Diagnostic Imaging and Nuclear Medicine Kyoto University Graduate School of MedicineKyoto 606-8507 Japan

AIM: To investigate the usefulness of branched-chain amino acids (BCAA) before transarterial chemoembolization (TACE) or radiofrequency ablation (RFA).

关键词： Branched-chain amino acids Cirrhosis Hepatocellular carcinoma Transarterial chemoembolization Radiofrequency ablation Hypoalbuminemia

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Crystallization of Cellobiohydrolase in the Presence of Cellulose-Degraded Cellobiose: Analysis of Intermolecular Interactions and Association Dynamics

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Journal of Crystallization Process and Technology 2014年第1期4卷 1-13页

作者： Kazuo Onuma Naoki Furubayashi Fujiko shibata Yoshiko Kobayashi Sachiko kaito Yuki Ohnishi Koji Inaka Maruwa Foods and Biosciences Inc. Tsutsui-cho Yamatokoriyama Nara Japan National Institute of Advanced Industrial Science and Technology (AIST) Tsukuba Ibaraki Japan

Crystallization of enzymes in presence of impurities is important for clarifying the role of enzymes in natural world. Although it is proposed that impurities inhibit nucleation of enzyme crystallization, details are unclear. In this study, crystallization of cellobiohydrolase from Aspergillus niger was investigated by dynamic and time-resolved static light scattering using cellobiose as an impurity. We aimed to clarify how cellobiose inhibits cellobiohydrolase crystallization and to crystallize cellobiohydrolase in concentrated cellobiose without using seeds. The contribution of attractive forces to total intermolecular interactions of cellobiohydrolase monomers increased with the molar ratio of cellobiose/cellobiohydrolase (R(cb/ce)). Association dynamics of cellobiohydrolase using lithium sulfate, however, showed that the initial aggregation rate decreased with an increase in R(cb/ce). Because binding sites of cellobioses to cellobiohydrolase molecules differed from those for the growth of protein crystals, the binding of cellobioses would increase the chemical potential of the cellobiohydrolase monomers, which gradually reduced supersaturation for growth as the aggregate size increased. This result was in contrast with the conventional idea that cellobiose inhibits the nucleation of cellobiohydrolase crystals. Gentle agitation of cellobiose-containing cellobiohydrolase solutions during sitting-drop vapor-diffusion growth resulted in the growth of cellobiohydrolase single crystals for all R(cb/ce) conditions without using seeds.

关键词： Enzyme Crystallization Inhibitor Hamaker Constant Light Scattering

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