Selective abolition of pancreatic RNase binding to its inhibitor protein

Selective abolition of pancreatic RNase binding to its inhibitor protein.

We have modified RNase inhibitor (RI) protein so that it no longer detectably binds pancreatic RNases but retains near-native affinity for human angiogenin (ANG). The K(i) value for RNase A is increased by a factor of >10(8), from 36 fM to >4 microM, and the selectivity factor for ANG is now >10(9). This dramatic change was achieved by remodeling the human RI loop segment Cys-408 -Leu-409 -Gly-...

Role of mammalian RNase inhibitor in cell-free protein synthesis.

Addition of the human placental RNase inhibitor at 10 mu/ml to a mixture of wheat germ extract and translation components, prior to the addition of mRNA from dog pancreas or influenza virus-infected cells, resulted in a significant increase in the yield of proteins synthesized. Analysis of the translation products by sodium dodecyl sulfate/polyacrylamide gel electrophoresis indicated that the i...

Complement Inhibitor C4b-Binding Protein

Silver Resistance In Acinetobacter baumannii BL54 Occurs Through Binding to a Ag-Binding Protein

The mechanism of plasmid mediated silver (Ag) resistance was investigated in Acinetobacter baumanniiBL54. The intracellular accumulation of Ag in both original strain BL54 and Escherichia coli K12transconjugant containing plasmid pUPI276 began immediately and reached a maximum within 60 minutes.This initial accumulation was followed by net loss of Ag which reached a maximum wi...

Binding of mitochondrial ATPase from ox heart to its naturally occurring inhibitor protein: localization by antibody binding.

The naturally occurring ATPase inhibitor protein from ox heart mitochondria was cross-linked to its binding site on the mitochondrial ATPase using 1-ethyl-3-(dimethylamino)propyl carbodiimide. The cross-linked product, when transferred electrophoretically to a nitrocellulose sheet, reacted with antibodies directed against the inhibitor protein and the beta-subunit of the ATPase. It was conclude...