Structural studies on human type IV collagen.

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چکیده

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Structural studies on human type IV collagen.

Type IV collagen was isolated from limited pepsin digests of human placenta by selective salt precipitation at acidic and neutral pH. The native protein was resistant to human skin collagenase but was cleaved by a rat mast cell protease. Molecular sieve chromatography of the reduced and alkylated material separated relatively homogeneous components of molecular weight 140,000 (140K) and 100,000...

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Collagen prolyl 4-hydroxylase (C-P4H) catalyses the formation of 4-hydroxyproline in collagens. Hydroxylation of prolines in –X-Pro-Glysequences is necessary for the formation of stable collagen triple helices. Molecular oxygen, Fe, 2-oxogluterate and ascorbate are required for the reaction [1]. In vertebrates C-P4H is an 2 2 tetramer in which is the catalytic subunit and the subunit is identic...

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Maternal Nexposure on Collagen Type Iv Pulmonary Changes in Mouse Offspring's

Purpose: In this study we evaluated the effect of maternal nicotine administration during pre and postnatal period on collagen IV changes in lung of mouse newborns. Materials and Methods: Female Balb/C mice were mated and finding vaginal plug was assumed as day zero of pregnancy. Pregnant mice, were divided into 2 experimental and 2 control groups. Experimental group 1, received 3 mg/kg nicotin...

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Human granulosa cells express integrin alpha2 and collagen type IV: possible involvement of collagen type IV in granulosa cell luteinization.

Previously, it has been shown that integrin alpha6beta1 expressed on human granulosa cells regulates luteinization in co-operation with its ligand, laminin. In this study, integrin alpha2 was immunohistochemically demonstrated to be expressed on granulosa and large luteal cells. It was also detected on luteinizing theca interna cells after ovulation. Immunoreactive collagen type IV, which is on...

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Type IV collagen-degrading enzyme activity was detected in human serum. Serum was preincubated with 4-aminophenylmercuric acetate and trypsin to activate the enzyme prior to assay. Type IV collagen, purified from human placentas and radiolabeled with [1-14C] acetic anhydride, was used as the substrate. The enzyme activity was measured at pH 7.5 and inhibited by treatment with ethylenediaminetet...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1979

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)83601-3