Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Sharon E. Porter"'
Autor:
Michael Landt, Sharon E. Porter, Allan S. Jaffe, James W. Grant, Charles E. Canter, Russel Hirsch, Jack H. Ladenson, Yvonne Landt
Publikováno v:
The Journal of Pediatrics. 130:872-877
Objective: To establish normal values and determine the impact of congenital or acquired heart disease on serum cardiac troponin I (cTnI). Methods: Concentrations of cTnI were measured in two groups of children. Group A represented ambulatory pediatr
Publikováno v:
Clinical Chemistry. 38:2203-2214
To improve the specificity of biochemical markers of myocardial infarction (MI), we have developed a double monoclonal "sandwich" enzyme immunoassay to measure cardiac troponin-I (cTnI) in serum. We produced eight IgG monoclonal antibodies against hu
Publikováno v:
Clinical Chemistry. 37:1356-1364
Myoglobin (Mb) is considered a useful marker for early detection of myocardial infarction and for monitoring cardiac reperfusion after thrombolytic therapy. We developed eight monoclonal antibodies to human cardiac Mb, characterized their epitopic re
Publikováno v:
Analytical biochemistry. 194(2)
Specific anti-calmodulin rabbit polyclonal and murine monoclonal antibodies have been produced with a thyroglobulin-linked peptide corresponding to amino acids 128-148 of bovine brain calmodulin. The monoclonal antibody is IgG-1 with kappa light chai
Autor:
Sharon E. Porter, Russel Hirsch, Michael Landt, James W. Grant, Jack H. Ladenson, Allan S. Jaffe, Ybonne Landt, Charles E. Canter
Publikováno v:
Clinical Biochemistry. 28:360
Autor:
Yvonne Landt, Sharon E. Porter, Hemant C. Vaidya, David N. Dietzler, Jack H. Ladenson, D. P. Silva
Publikováno v:
Clinical Chemistry. 34:2410-2414
We have developed a rapid, one-step assay for measuring lactate dehydrogenase-1 (LD-1) activity in serum after extraction of LD-2, LD-3, LD-4, and LD-5 isoenzymes by an immobilized M-subunit-specific monoclonal antibody (D.8.1). In the assay, 100 mic
Publikováno v:
Biochemical and Biophysical Research Communications. 122:289-296
We show that physiological concentrations of GTP can significantly inhibit wild-type Escherichia coli ADP-glucose synthetase (the rate-limiting enzyme of bacterial glycogen synthesis) and that mutant-strain enzymes known to show less inhibition by ph
Autor:
Moon H. Nahm, Sharon E. Porter, Curtis A. Parvin, C Amyx, David N. Dietzler, Gerald Kessler, Yvonne Landt, K Whalen, Adrain C. McClellan, Hemant C. Vaidya
Publikováno v:
Clinical Chemistry. 34:575-581
This semi-automated colorimetric assay for the MB isoenzyme of creatine kinase (EC 2.7.3.2) is based on a monoclonal antibody ("Conan-MB") specific for this isoenzyme and is a modification of a previously published method (Vaidya et al., Clin Chem 19
Publikováno v:
Clinical Chemistry. 35:985-989
We describe a simple, rapid immunoaffinity procedure for purifying the MB isoenzyme of creatine kinase. Immunoaffinity gel is prepared by linking a monoclonal antibody ("Conan-MB"), specific for this isoenzyme, to Sepharose 4B. Heart tissue is homoge
Publikováno v:
Biochemical and Biophysical Research Communications. 99:1433-1442
In Escherichia coli an abrupt increase in the rate of glycogen synthesis occurs at the onset of total nitrogen starvation. We present here both in vivo and in vitro data indicating that this increase occurs because of the loss of a nitrogen-containin