Thermal Denaturation of β-Connectin Isolated from Carp Muscle

Thermal denaturation of A-DNA

The DNA molecule can take various conformational forms. Investigations focus mainly on the so-called ‘B-form’, schematically drawn in the famous paper by Watson and Crick [1]. This is the usual form of DNA in a biological environment and is the only form that is stable in an aqueous environment. Other forms, however, can teach us much about DNA. They have the same nucleotide base pairs for ‘bui...

Connectin filaments in stretched skinned fibers of frog skeletal muscle

Indirect immunofluorescence microscopy of highly stretched skinned frog semi-tendinous muscle fibers revealed that connectin, an elastic protein of muscle, is located in the gap between actin and myosin filaments and also in the region of myosin filaments except in their centers. Electron microscopic observations showed that there were easily recognizable filaments extending from the myosin fil...

Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.

Maltodextrin phosphorylase from Escherichia coli (MalP) is a dimeric protein in which each approximately 90-kDa subunit contains active-site pyridoxal 5'-phosphate. To unravel factors contributing to the stability of MalP, thermal denaturations of wild-type MalP and a thermostable active-site mutant (Asn-133-->Ala) were compared by monitoring enzyme activity, cofactor dissociation, secondary st...

Thermal denaturation of DNA from bromodeoxyuridine substituted cells

The thermal denaturation of DNA from cell lines extensively substituted with bromodeoxyuridine has been examined spectrophotometrically over a wide range in ionic strength and by thermal elution from hydroxyapatite columns. BrdU substitution stabliizes DNA at all ionic strengths between 7.5 mM and 1350 mM potassium ion concentration, although a plot of log ionic strength vs Tm deviates from lin...

Irreversible thermal denaturation of Glucose oxidase from Aspergillus niger