Spermine and spermidine act as chemical chaperones and enhance chaperone-like and membranolytic activities of major bovine seminal plasma protein, PDC-109
The major bovine seminal plasma protein, PDC-109, binds to choline phospholipids of the
sperm plasma membrane and induces an efflux of cholesterol and choline phospholipids …
sperm plasma membrane and induces an efflux of cholesterol and choline phospholipids …
Contrasting effects of molecular crowding on the membrane-perturbing and chaperone-like activities of major bovine seminal plasma protein, PDC-109
Crowded environments inside cells and biological fluids greatly affect protein stability and
activity. PDC-109, a polydisperse oligomeric protein of the bovine seminal plasma …
activity. PDC-109, a polydisperse oligomeric protein of the bovine seminal plasma …
Purification, molecular characterization and ligand binding properties of the major donkey seminal plasma protein DSP-1
Fibronectin type-II (FnII) family proteins are the major proteins in many mammalian species
including bull, horse and pig. In the present study, a major FnII protein has been identified …
including bull, horse and pig. In the present study, a major FnII protein has been identified …
Probing the chemical unfolding and phospholipid binding to the major protein of donkey seminal plasma, DSP-1 by fluorescence spectroscopy
Fibronectin type-II (FnII) proteins which constitute the major fraction in the seminal plasma of
many mammals, bind to choline phospholipids on the spermatozoa and play a crucial role in …
many mammals, bind to choline phospholipids on the spermatozoa and play a crucial role in …
Glycosylation differentially modulates membranolytic and chaperone-like activities of PDC-109, the major protein of bovine seminal plasma
BP Singh, RS Sankhala, A Asthana… - Biochemical and …, 2019 - Elsevier
The major bovine seminal plasma protein, PDC-109, is a mixture of glycosylated (BSP-A1)
and non-glycosylated (BSP-A2) isoforms of a 109-residue long polypeptide. It binds to …
and non-glycosylated (BSP-A2) isoforms of a 109-residue long polypeptide. It binds to …
Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone‐like activities of bovine seminal plasma protein PDC‐109
The fibronectin type II (FnII) domain, present in diverse vertebrate proteins, plays crucial
roles in several fundamental biological processes. PDC‐109, the major bovine seminal …
roles in several fundamental biological processes. PDC‐109, the major bovine seminal …
Thermodynamic analysis of protein–lipid interactions by isothermal titration calorimetry
Isothermal titration calorimetry is a highly sensitive and powerful technique for the study of
molecular interactions. This method can be applied universally for studying the interaction …
molecular interactions. This method can be applied universally for studying the interaction …
Low-pH Molten Globule-Like Form of CIA17, a Chitooligosaccharide-Specific Lectin from the Phloem Exudate of Coccinia indica, Retains Carbohydrate-Binding …
pH-induced changes in the conformation, structural dynamics, and carbohydrate-binding
activity of Coccinia indica agglutinin (CIA17), a PP2-type lectin, were investigated employing …
activity of Coccinia indica agglutinin (CIA17), a PP2-type lectin, were investigated employing …
Primary structure determination and physicochemical characterization of DSP-3, a phosphatidylcholine binding glycoprotein of donkey seminal plasma
Major proteins of the seminal plasma in a variety of mammals such as bovine PDC-109,
equine HSP-1/2, and donkey DSP-1 contain fibronectin type-II (FnII) domains and are …
equine HSP-1/2, and donkey DSP-1 contain fibronectin type-II (FnII) domains and are …
Differential modulation of the chaperone-like activity of HSP-1/2, a major protein of horse seminal plasma by anionic and cationic surfactants
The major protein of equine seminal plasma, HSP-1/2 exhibits chaperone-like activity (CLA)
by protecting various target proteins against thermal, chemical and oxidative stress …
by protecting various target proteins against thermal, chemical and oxidative stress …