Abstract:
:Treatment of a 128 kDa mouse nardilysin with trypsin initially produced an active 105 kDa N-terminally cleaved form. Continued trypsin digestion occurred at the C-terminus, producing inactive core species of approximately 92, 76.5, and 62 kDa. Protease V8 digestion generated a stable approximately 105 kDa form, nardilysin(V8), that was cleaved near the N-terminal trypsin site. The approximately 105 kDa nardilysin(V8) exhibited the same K(m) as did the uncleaved enzyme for substrates of the type Abz-GGFX(1)X(2)X(3)VGQ-EDDnp, where X residues were varied. However, k(cat) for nardilysin(V8) was 5-6 times greater. Both uncleaved nardilysin and nardilysin(V8) are inhibited by NaCl; however, nardilysin(V8) exhibits an IC(50) of approximately 2 mM compared to an IC(50) of approximately 50 mM for uncleaved nardilysin. Nardilysin(V8) is more sensitive to inhibition by phosphate buffer. Treatment of nardilysin(V8) with trypsin generated primarily the 92 kDa form which was inactive. Attempts to express nardilysin as a 105 kDa truncated N-terminal form or as a C-terminally truncated form led to inactive proteins.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Ma Z,Chow KM,Csuhai E,Hersh LBdoi
10.1016/S0003-9861(02)00020-6subject
Has Abstractpub_date
2002-05-15 00:00:00pages
198-204issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(02)00020-6journal_volume
401pub_type
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章,评审
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1995-07-10 00:00:00
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1993.1146
更新日期:1993-03-01 00:00:00