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Pancreatic trypsin activates human promatrix metalloproteinase-2
Rune I. Lindstad
, Ingebrigt Sylte
,
Svein-Ole Mikalsen
, Per O. Seglen
, Eli Berg
, Jan-Olof Winberg
Research output
:
Contribution to journal
›
Article
›
peer-review
25
Citations (Scopus)
Overview
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Dive into the research topics of 'Pancreatic trypsin activates human promatrix metalloproteinase-2'. Together they form a unique fingerprint.
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Biochemistry, Genetics and Molecular Biology
Metalloproteinase
100%
Metalloendopeptidase
100%
Gelatinase A
100%
MMP2
100%
C-Terminus
60%
Catalytic Efficiency
60%
Enzyme
40%
Membrane-Type Matrix Metalloproteinase-1
40%
Metalloprotease Inhibitor
40%
N-Terminus
40%
Solution and Solubility
20%
Matrix-Assisted Laser Desorption-Ionization
20%
Turnover Number
20%
Time-of-Flight Mass Spectrometry
20%
Steady State
20%
Polidocanol
20%
Keyphrases
Trypsin
100%
Matrix metalloproteinase-2 (MMP-2)
100%
Kcat
33%
Enzyme-activated
16%
Tissue Inhibitor of metalloproteinase-1 (TIMP-1)
16%
Terminal Residue
16%
MT1-MMP
16%
Environmental Factors
8%
C-terminal Truncation
8%
Regulatory Potential
8%
Kinetic Coefficients
8%
Truncation
8%
Km Value
8%
Catalytic Potential
8%
Steady-state Kinetics
8%
Docking Studies
8%
Sequential Processing
8%
Weak Binding
8%
Physiologic
8%
Proenzymes
8%
Tissue Inhibitor of Matrix metalloproteinase-2
8%
Ca2+
8%
56 kDa
8%
Active Form
8%
Active Species
8%
Brij-35
8%
MALDI-TOF Analysis
8%
N-terminus
8%