[The fluorescence of pepsin conjugates with DNS-chloride].
Parameters of rotational relaxation of pepsin conjugated in neutral and slightly alkaline solutions with a fluorescent label 1-dimethylaminonaphthalene-5-sulphonyl chloride (DNS-Cl) are measured by a fluorescence polarization method. It is shown that the globule of pepsin denatured and loose at lakaline pH values converts into a compact form after transfer to acidic solution. The compactness of this new form is close to that of native inhibited pepsin. A new globule is distinguished from the native by the absence of segmental flexibility. Conjugated with a DNS at pH less than or equal to 7.0 pepsin relaxes in solution as catalytically active dansylated aminopepsin (DNS-3-aminotyrosine pepsin). Evidence is presented that these conjugates are also characterized by segmental flexibility.
D000818:Animals; D002712:Chlorides; D003619:Dansyl Compounds; D005453:Fluorescence; D006863:Hydrogen-Ion Concentration; D010434:Pepsin A; D013552:Swine
D002712:Chlorides; D003619:Dansyl Compounds; D010434:Pepsin A
Issledovania fluorestsentsii kon''iugatov pepsina s DNK-khloridom