Search results for "Disulfide bonds"
showing 3 items of 3 documents
Maternal Inheritance of a Recessive RBP4 Defect in Canine Congenital Eye Disease
2018
SUMMARY Maternally skewed transmission of traits has been associated with genomic imprinting and oocyte-derived mRNA. We report canine congenital eye malformations, caused by an amino acid deletion (K12del) near the N terminus of retinol-binding protein (RBP4). The disease is only expressed when both dam and offspring are deletion homozygotes. RBP carries vitamin A (retinol) from hepatic stores to peripheral tissues, including the placenta and developing eye, where it is required to synthesize retinoic acid. Gestational vitamin A deficiency is a known risk factor for ocular birth defects. The K12del mutation disrupts RBP folding in vivo, decreasing its secretion from hepatocytes to serum. T…
Characterization of sulfhydryl oxidase from Aspergillus tubingensis
2017
Background Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. Results The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initia…
Electrochemical modifications of proteins: disulfide bonds reduction
2002
International audience; Electrochemical reduction of lysozyme disulfide bonds was achieved at pH between 10 and 11.Below pH 10, no disulfide bond cleavage was observed. At pH higher than 12, the cleavage of disulfide bonds is essentially due to hydrolysis. The addition of denaturant considerably enhanced the performance of the electrochemical device.