Collagen fibril formation in the presence of sodium dodecyl sulphate

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Collagen fibril formation in the presence of sodium dodecyl sulphate.

Sodium dodecyl sulphate (SDS) was used to weaken both the electrostatic and the hydrophobic interactions during collagen fibrillogenesis in vitro. The rate and extent of fibril formation as well as fibril morphology were affected by SDS concentration. Both the formation of large fibrils at 0.3 mM-SDS and the complete cessation of fibril formation at 0.5 mM-SDS were considered to be the result o...

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Thermal Analysis of Adenosine Deaminase in the Presence of Sodium N-Dodecyl Sulphate

The thermal denaturation of adenosine deaminase (ADA) has been investigated in the presence of sodium n-dodecyl sulphate (SDS) over the temperature range of (293-363K) in 2.5 mM phosphate buffer, pH 6.4 by temperature scanning spectroscopy. The interaction of SDS caused the folding of adenosine deaminanse resulting in a decrease of TH (temperature of minimum solubility), TS<...

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thermal denaturation of α-amylase from bacillus amyloliquefaciens in the presence of sodium dodecyl sulphate*

the thermal denaturation of α-amylase from bacillus amyloliquefaciens has been investigated in the presence and absence of sodium dodecyl sulphate (sds) over the temperature range (293-373) k in 20 mm sodium phosphate buffer, ph 6.9, using temperature scanning spectroscopy. the presence of sds caused the destabilization of α-amylase resulting in a decrease in the temperature of unfolding with a...

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thermal analysis of adenosine deaminase in the presence of sodium n-dodecyl sulphate

the thermal denaturation of adenosine deaminase (ada) has been investigated in the presence of sodium n-dodecyl sulphate (sds) over the temperature range of (293-363k) in 2.5 mm phosphate buffer, ph 6.4 by temperature scanning spectroscopy. the interaction of sds caused the folding of adenosine deaminanse resulting in a decrease of th (temperature of minimum solubility), ts (temperature of maxi...

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Sodium dodecyl sulphate electrophoresis of wheat gliadins.

Polypeptide chain weights of a-, 8and y-gliadin fractions have been estimated by polyacrylamide gel electrophoresis in the presence of mercaptoethanol and sodium dodecyl sulphate. Values lie in the range 32 000 to 44 OOO. When available data on the amino acid analyses were adjusted and compared, significant similarities emerged. It is suggested that these gliadins contain a minimum of 4 cystine...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1985

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2280551