Collagen in the human lung. Quantitation of rates of synthesis and partial characterization of composition.

作者: K Bradley , S McConnell-Breul , R G Crystal

DOI: 10.1172/JCI107961

关键词:

摘要: The presence of collagen in lung is fundamental normal structure and function. Methods have been developed to examine human fetal adult with respect its composition synthesis. second trimester has a large number cells per unit mass (36.6 plus or minus 2.7 mug DNA/mg dry wt) relatively small amounts (17.0 5.3 collagen/mg wt). the (11.1 3.4 30% lung, but 11 times more (196 25 can be partially characterized by extraction salt at neutral pH, acetic acid, guanidine. extracted chains, representing 10% total collagen, chromatograph as alpha1 alpha2 each mol wt 100,000 an animo acid characteristic for not specific lung. Short-term explant cultures synthesize alpha chains which isolated ion-exchange chromatography. These 30-40% synthesized explants, coelectrophorese on acrylamide gels: they are destroyed clostridial collagenase 100,000. Although these explants only characterized, rate synthesis both noncollagen protein quantitated. In 4.0 1.2% amino acids incorporated into hour collagen. this percentage (4.2 0.9%) remarkably similar. values almost identical relative rabbit same age range. This technology should applicable answer questions regarding degradation disease.

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