Heat Stability of Bovine Lactoferrin at Acidic pH
نویسندگان
چکیده
منابع مشابه
Molecular Dynamics Simulations Capture the Misfolding of the Bovine Prion Protein at Acidic pH
Bovine spongiform encephalopathy (BSE), or mad cow disease, is a fatal neurodegenerative disease that is transmissible to humans and that is currently incurable. BSE is caused by the prion protein (PrP), which adopts two conformers; PrPC is the native innocuous form, which is α-helix rich; and PrPSc is the β-sheet rich misfolded form, which is infectious and forms neurotoxic species. Acidic pH ...
متن کاملA SPECTROSCOPIC STUDY ON THE HEAT INDUCED CHANGES OF GLUCOSE OXIDASE AT ACIDIC pH VALUES
The heat induced conformational and structural changes of glucose oxidase from Aspergillus niger at pH 5.0 and 4.0 were investigated using fluorescence spectroscopy. Experimental studies were conducted in buffer solution in the 25°C70°C temperature range at constant time. At both pH values, the phase diagram was linear, indicating the presence of two molecular species induced by thermal treatme...
متن کاملMonomeric Banana Lectin at Acidic pH Overrules Conformational Stability of Its Native Dimeric Form
Banana lectin (BL) is a homodimeric protein categorized among jacalin-related family of lectins. The effect of acidic pH was examined on conformational stability of BL by using circular dichroism, intrinsic fluorescence, 1-anilino-8-napthalene sulfonate (ANS) binding, size exclusion chromatography (SEC) and dynamic light scattering (DLS). During acid denaturation of BL, the monomerization of na...
متن کاملAssociation of Bovine Lactoferrin Gene with Mastitis in Frieswal Cattle
ThirtyFrieswal lactating cows were screened for clinical and subclinical mastitis and subsequently classified into healthy, subclinically affected and clinically affected groups each group comprising of 10 cows. Polymorphism of cow lactoferrin (LTF) gene promoter was determined by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP). The results showed that LFT gene pro...
متن کاملA stability transition at mildly acidic pH in the alpha-hemolysin (alpha-toxin) from Staphylococcus aureus.
The effects of mildly acidic conditions on the free energy of unfolding (DeltaG(u)(buff)) of the pore-forming alpha-hemolysin (alphaHL) from Staphylococcus aureus were assessed between pH 5.0 and 7.5 by measuring intrinsic tryptophan fluorescence, circular dichroism and elution time in size exclusion chromatography during urea denaturation. Decreasing the pH from 7.0 to 5.0 reduced the calculat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 1991
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(91)78144-7