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Biochemical and biophysical studies of reactive center cleaved plasminogen activator inhibitor type 1. The distance between P3 and P1' determined by donor-donor fluorescence energy transfer.
J Biol Chem
August 1996
Department of Medical Biochemistry and Biophysics, Umeâ University, S-901 87 Umeâ, Sweden.
Plasminogen activator inhibitor type 1 (PAI-1) is a fast acting inhibitor of plasminogen activators (PAs). In accordance with other serpins, PAI-1 is thought to undergo a conformational change upon reactive center cleavage. In this study we have developed methods to produce and purify reactive center cleaved wild-type PAI-1 and characterized this molecular form of PAI-1 by biochemical and biophysical methods.
View Article and Find Full Text PDFPhosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase. Inhibition of factor I-mediated cleavage of C3b.
J Immunol
June 1995
Department of Medical and Physiological Chemistry, University of Uppsala, Sweden.
Phosphorylation of C3 in vitro has been shown previously to lead to significantly altered function of the protein. Platelets are known to contain and release considerable amounts of protein kinases and ATP, which are prerequisites for protein phosphorylation. The aim of the present study was to investigate whether C3 is phosphorylated extracellularly by human platelets.
View Article and Find Full Text PDFInhibition and affinity chromatography of chicken lung angiotensin I-converting enzyme with captopril.
Comp Biochem Physiol B
July 1992
Departamento de Bioquímica, Biología Molecular y Fisiologia, Facultad de Ciencias, Universidad de Valladolid, Spain.
1. Angiotensin I-converting enzyme (EC 3.4.
View Article and Find Full Text PDFProrenin-renin axis in synovial fluid in patients with rheumatoid arthritis and osteoarthritis.
Endocrinol Jpn
June 1992
Third Department of Internal Medicine, Gifu University School of Medicine, Japan.
This study was undertaken 1) to determine whether or not renin is present in synovial fluid in patients with rheumatoid arthritis and osteoarthritis, and, if present, 2) to investigate whether it is synthesized in synovial fluid, or it is only transported from the circulation into the synovial cavity. The active renin concentration (indirect) was measured with angiotensin I radioimmunoassay kits. Inactive renin was converted into active renin with Sepharose-bound trypsin.
View Article and Find Full Text PDFCharacterization of metalloproteinases and tissue inhibitors of metalloproteinases in human plasma.
Connect Tissue Res
January 1993
Department of Research, Department of Veterans Affairs Medical Center, Northport, New York 11768.
In this study, we have identified and characterized metalloproteinases and tissue inhibitors of metalloproteinases (TIMPs) in human plasma. Treatment of plasma with trypsin or aminophenylmercuric acetate resulted in activation of latent gelatinolytic activity. Fractionation of plasma by gelatin Sepharose chromatography resulted in the isolation of 72 kDa and 92 kDa gelatinases/type IV collagenases.
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