Detail of "70671-54-4"

Reference

L- and D-N2-benzyloxycarbonyllysine

L- and D-N2-benzyloxycarbonyllysine. Fujino, Toshihiro; Kato, Takashi; Matsukuma, Yoshihisa (Toray Industries, Inc., Japan). Jpn. Kokai Tokkyo Koho JP 62005942 A2 12 Jan 1987 Showa, 3 pp. (Japan) CODEN: JKXXAF. CLASS: ICM: C07C101-24. ICS: C07C099-06. APPLICATION: JP 85-145258 2 Jul 1985. DOCUMENT TYPE: Patent CA Section: 34 (Amino Acids, Peptides, and Proteins) Title compds. were prepd. by hydrolysis of L- and D-a-benzyloxycarbonylamino-e-caprolactam. Thus, L-a-benzyloxycarbonylamino-e-caprolactam was hydrolyzed in 1N HCl at 90° for 12 h to give 60% N2-benzyloxycarbonyl-L-lysine.Except for chemicals metioned above, 103478-12-2 and 70671-54-4 are also used. .

Enantioselective enzymatic cleavage of N-benzyloxycarbonyl groups

Enantioselective enzymatic cleavage of N-benzyloxycarbonyl groups. Patel, Ramesh N.; Nanduri, Venkata; Brzozowski, David; McNamee, Clyde; Banerjee, Amit (Process Research & Development, Pharmaceutical Research Institute, Bristol-Myers Squibb, New Brunswick, NJ 08903, USA). Advanced Synthesis & Catalysis, 345(6+7), 830-834 (English) 2003 Wiley-VCH Verlag GmbH & Co. KGaA. CODEN: ASCAF7.Several reagents with their cas registry numbers 87797-02-2 and 70671-54-4 are used here. ISSN: 1615-4150. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) Section cross-reference(s): 7 A new enzymic process for the enantioselective cleavage of N-benzyloxycarbonyl (Cbz) groups from protected amino acids and related compds. has been developed. The Cbz-deprotecting enzyme was isolated from cell exts. of Sphingomonas paucimobilis SC 16113 and purified to homogeneity. The purified protein has a mol. wt. of 155,000 daltons and a subunit size of 44,000 daltons. .