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Improvement of catalytic antibody activity by protease processing

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
315
Issue
3
Identifiers
DOI: 10.1016/j.bbrc.2004.01.094
Keywords
  • Catalytic Antibody
  • Bence Jones Proteins
  • Catalytic Activity
  • Immunoglobulin L Chain
  • Vl
Disciplines
  • Biology

Abstract

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 K m and k cat values of Chromozym TRY hydrolysis for HIR were 1.5 × 10 −4 M and 6.2 min −1, and for the VL fragment 7.3 × 10 −4 M and 4.8 × 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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