Ohara Kyoko, Munakata Hiroshi, Hifumi Emi, Uda Taizo, Matsuura Kinji
Kinki University School of Medicine, Japan.
Biochem Biophys Res Commun. 2004 Mar 12;315(3):612-6. doi: 10.1016/j.bbrc.2004.01.094.
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.
一种免疫球蛋白轻链（HIR）用赖氨酰内肽酶处理。对消化混合物进行凝胶过滤色谱分析，发现一个峰，其比原始样品显示出显著更高的比催化活性。该峰中的蛋白质大小为11 kDa，构成HIR的VL片段。HIR对Chromozym TRY水解的Km和Kcat值分别为1.5×10⁻⁴ M和6.2 min⁻¹，而VL片段的Km和Kcat值分别为7.3×10⁻⁴ M和4.8×10² min⁻¹。本文研究的五个BJP中有三个在用赖氨酰内肽酶处理后显示出催化活性升高。完整抗体也得到了类似的结果。
