Native, denatured, performic acid-oxidized or S-sulfo insulin and S-sulfo or performic acid-oxidized A- and B-chains were digested with subtilisin type Carsberg. The proteolysis was followed by measuring the uptake of alkali through autotitration. The kinetic study shows the existence of 2 first-order reaction classes which differ markedly in rate constant. The number of bonds split with fast and with slow reactions has been calculated. Only one of a total of 12 cleavable bonds in native insulin is opened by fast reaction. In the denatured protein the number of bonds split by the fast reaction increases to 4 and in the oxidized and S-sulfo protein 3 bonds are cleaved, while the slow cleavable bonds number 2 and 7, respectively, The kinetic study of the proteolysis of S-sulfo A-chain and of oxidized or S-sulfo B-chain shows that two bonds are split in A-chain with the fast and slow reactions, while in B-chain only one of the six cleavable bonds is susceptible to fast attack.
Autori interni: | ||
Autori: | RONCA G; MONTALI U; LUCACCHINI A; RONCATESTONI S; ROSSI CA | |
Titolo: | DIGESTION OF INSULIN DERIVATIVES WITH SUBTILISIN - KINETIC STUDY | |
Anno del prodotto: | 1975 | |
Appare nelle tipologie: | 1.1 Articolo in rivista |