Results 311 to 320 of about 87,970 (343)
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Nihon rinsho. Japanese journal of clinical medicine, 1995
Elastases are unique among the proteases in that they are capable of hydrolyzing the scleroprotein elastin. The enzymes include pancreatic elastases 1 (Protease E) and 2, and neutrophil elastase. These three elastases also have esterase and amidase activity toward synthetic substrates such as succinyl-trialanine-p-nitroanilide.
T, Hayakawa +3 more
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Elastases are unique among the proteases in that they are capable of hydrolyzing the scleroprotein elastin. The enzymes include pancreatic elastases 1 (Protease E) and 2, and neutrophil elastase. These three elastases also have esterase and amidase activity toward synthetic substrates such as succinyl-trialanine-p-nitroanilide.
T, Hayakawa +3 more
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Annual Review of Medicine, 1985
This article surveys elastinolytic proteinases in man, excluding enzymes of the pancreas and digestive tract. Special emphasis is placed on the elastase of polymorphonuclear neutrophils (PMN). The properties of this latter enzyme, its target molecules in plasma and connective tissues, and its endogenous regulators are briefly discussed.
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This article surveys elastinolytic proteinases in man, excluding enzymes of the pancreas and digestive tract. Special emphasis is placed on the elastase of polymorphonuclear neutrophils (PMN). The properties of this latter enzyme, its target molecules in plasma and connective tissues, and its endogenous regulators are briefly discussed.
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Nature, 1960
SINCE Balo and Banga1 described the pancreatic enzyme elastase, its dissolving effect on elastin, and its possible implications in atherosclerosis, a considerable amount of interest has been focused on the quantitative measurement of its enzymatic activity.
Robert F. Gilfillan +2 more
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SINCE Balo and Banga1 described the pancreatic enzyme elastase, its dissolving effect on elastin, and its possible implications in atherosclerosis, a considerable amount of interest has been focused on the quantitative measurement of its enzymatic activity.
Robert F. Gilfillan +2 more
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Levels of elastase activity in bronchoalveolar lavage fluids of healthy smokers and nonsmokers.
American Review of Respiratory Disease, 2015Elastase activity was measured in concentrated, cell-free bronchoalveolar lavage (BAL), using the synthetic substrate butyloxycarbonyl-L-alanyl-L-alanyl-L-prolyl-L-valyl-amino-methylcoumarin.
A. Janoff, L. Raju, R. Dearing
semanticscholar +1 more source
Solubilized elastin as a substrate for elastase and elastase inhibitor determinations
Biochemical Medicine, 1971Abstract This paper describes a test for elastase which employs oxalic acid-solubilized elastin as the substrate. The test described is more sensitive than those using insoluble elastin-dye complexes and more specific than the recently introduced tests using synthetic peptide-esters.
Ines Mandl, Stephen Keller
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American Review of Respiratory Disease, 2015
Evidence obtained by biochemical analysis of BAL fluids from patients with ARDS indicates that at least two important pathogenic events take place in the pulmonary tissues. These are the release of elastase from neutrophils and the generation of oxidants.
C. Cochrane +4 more
semanticscholar +1 more source
Evidence obtained by biochemical analysis of BAL fluids from patients with ARDS indicates that at least two important pathogenic events take place in the pulmonary tissues. These are the release of elastase from neutrophils and the generation of oxidants.
C. Cochrane +4 more
semanticscholar +1 more source
Digestion of elastin by porcine pancreatic elastase I and elastase II
International Journal of Peptide and Protein Research, 1985Elastin was fully solubilized by digestion with elastase I or elastase II. Each digest was separated into high‐molecular weight and low‐molecular weight fractions that were characterized by the correspondence to their amino acid content, N‐terminal sequence and C‐terminal amino acids. It was found that although the relative amount of amino acids in the
Arieh Gertler, Yigal Burstein, M. Vered
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The effect of lathyrogens on the evolution of elastase-induced emphysema.
American Review of Respiratory Disease, 2015When pancreastic elastase is introduced into the lungs of hamsters to produce emphysema, there is an initial rapid destruction of elastin followed by a subsequent resynthesis. In order to investigate its pathologic significance, we attempted to interfere
C. Kuhn, B. Starcher
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American Review of Respiratory Disease, 2015
The null-null phenotype of alpha 1-antitrypsin (alpha 1AT), a phenotype characterized by no detectable alpha 1AT in serum, presents a rare opportunity to examine the contribution of alpha 1AT to the antineutrophil elastase protection of the lower ...
M. Wewers, M. Casolaro, R. Crystal
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The null-null phenotype of alpha 1-antitrypsin (alpha 1AT), a phenotype characterized by no detectable alpha 1AT in serum, presents a rare opportunity to examine the contribution of alpha 1AT to the antineutrophil elastase protection of the lower ...
M. Wewers, M. Casolaro, R. Crystal
semanticscholar +1 more source
The Journal of Immunology, 1959
Summary Although crystalline elastase has a molecular weight of only 25,000, an antibody was obtained in rabbits injected with an elastase-adjuvant mixture. The antibody produced a precipitin reaction in vitro as well as passive anaphylaxis in guinea pigs.
B C, McIVOR, H D, MOON
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Summary Although crystalline elastase has a molecular weight of only 25,000, an antibody was obtained in rabbits injected with an elastase-adjuvant mixture. The antibody produced a precipitin reaction in vitro as well as passive anaphylaxis in guinea pigs.
B C, McIVOR, H D, MOON
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