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Keywords: Yamakawa T; Hakomori SI; highly cited paper EN Yamakawa T Hakomori SI highly cited paper 135 136 2 09/08/22 20220901 NES 220901 For the past decades, the field of biochemistry has undergone substantial changes from molecular levels to genomic levels and the use of high-technology, information-rich biochemistry and molecular biology promises to provide powerful and useful tools for use in new development by researchers in the future. J Biochem 55, 205 - 208 Google Scholar PubMed OpenURL Placeholder Text WorldCat 2 Yamakawa, T. (1996) A reflection on the early history of glycosphingolipids. Yamakawa T, Hakomori SI, highly cited paper. [Extracted from the article]

The Award Committee selects the winning papers from a shortlist made up of nominations from individual authors, as well as nominations put forward by a committee of JB Editorial Board members. The Japanese Biochemical Society has held the JB Award since 1993 with the aim of encouraging authors to submit more papers to the I Journal of Biochemistry i . B Quantitative nascent proteome profiling by dual-pulse labelling with O-propargyl-puromycin and stable isotope-labelled amino acids: b Junki Uchiyama, Yasushi Ishihama and Koshi Imami (volume 169, issue 2, February 2021, pages 227-236, https://doi.org/10.1093/jb/mvaa104). [Extracted from the article]

I would like to congratulate the Journal of Biochemistry (JB) on its 100th anniversary. I served as the Editor-in-Chief for four years starting in 2010 and succeeded Dr Naoyuki Taniguchi. [ABSTRACT FROM AUTHOR]

T7 system is a commonly used in protein expression and the highest transcription activity of T7 RNAP usually caused the instability of T7 system. In order to apply T7 system extensively, it is essential to characterize T7 RNAP activity. In the present paper, an assay method for T7 RNAP activity was developed with a transcription–translation (TX-TL) system. After the optimization of TX-TL system, the operating parameters were determined as 34°C, 60 min with 20 ng/μl of plasmid DNA template. The standard curve of TX-TL assay method indicated an excellent correlation (r  = 0.998), and the sensitivity was better than that of western blotting method. The precision investigation indicated a mean-relative error of 2.58% and a standard-relative error of 7.01%. Moreover, the cell lysate could be added directly to the optimized TX-TL system without affecting T7 RNAP activity assay. The feasibility of present method was further confirmed by characterizing T7 RNAP activity in cell lysate of five strains of Escherichia coli (E. coli) DH5α with different T7 RNAP activities and seven commercial strains of E. coli (DE3). The present assay method for T7 RNAP activity would have a great application in synthetic biology, metabolic engineering, enzyme engineering and biomedicine. [ABSTRACT FROM AUTHOR]