Literature DB >> 14975745

Improvement of catalytic antibody activity by protease processing.

Kyoko Ohara1, Hiroshi Munakata, Emi Hifumi, Taizo Uda, Kinji Matsuura.   

Abstract

An immunoglobulin L chain (HIR) was treated with lysyl-endopeptidase. Gel filtration chromatography of the digestion mix identified a peak displaying a significantly higher specific catalytic activity than that of the original sample. The protein in the peak was 11 kDa in size and constituted the VL fragment of HIR. The Km and Kcat values of Chromozym TRY hydrolysis for HIR were 1.5 x 10(-4) M and 6.2 min(-1), and for the VL fragment 7.3 x 10(-4) M and 4.8 x 10(2) min(-1), respectively. Three out of the five BJPs studied in this paper displayed elevated catalytic activity after processing with lysyl-endopeptidase. Similar results were also obtained for the complete antibody.

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Year:  2004        PMID: 14975745     DOI: 10.1016/j.bbrc.2004.01.094

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Biochemical features of a catalytic antibody light chain, 22F6, prepared from human lymphocytes.

Authors:  Emi Hifumi; Naoko Fujimoto; Mitsue Arakawa; Eri Saito; Shingo Matsumoto; Nobuyuki Kobayashi; Taizo Uda
Journal:  J Biol Chem       Date:  2013-05-15       Impact factor: 5.157

  1 in total

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