Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
نویسندگان
چکیده
A rapid and convenient method for peptide mapping of proteins has been developed. The technique, which is especially suitable for analysis of proteins that have been isolated from gels containg sodium dodecyl sulfate, involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis. The pattern of peptide fragments produced is characteristic of the protein substrate and the proteolytic enzyme and is highly reproducible. Several common proteases have been used including chymotrypsin, Staphylococcus aureus protease, and papain.
منابع مشابه
Peptide Mapping by Limited Proteolysis in Sodium Dodecyl Sulfate and Analysis by Gel
A rapid and convenient method for peptide mapping of proteins has been developed. The technique, which is especially suitable for analysis of proteins that have been isolated from gels containing sodium dodecyl sulfate, involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis. The pattern of pept...
متن کاملAltered form of placental alkaline phosphatase produced by JAR choriocarcinoma cells in culture.
The alkaline phosphatase activity expressed by JAR choriocarcinoma cells was compared to the placental isoenzyme of human alkaline phosphatase by several criteria. JAR cell alkaline phosphatase was similar to the placental isoenzyme with respect to heat and urea stability and sensitivity to most inhibitors, but it differed significantly from placental alkaline phosphatase in its sensitivity to ...
متن کاملProteolytic interconversion of electrophoretic variants of the enzyme rhodanese.
It has been confirmed that the enzyme rhodanese, although a homogeneous single polypeptide chain protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is separable by electrophoresis under nondenaturing conditions into four species which differ in net surface charge (I-IV in the order of increasing positive charge). Limited proteolysis can interconvert these species. Chymotrypsi...
متن کاملThree immunoidentical cytochromes P-450 from liver microsomes of phenobarbital-treated rats.
Three forms of cytochrome P-450 were purified to homogeneity from liver microsomes of Wistar-strain rats treated with phenobarbital. They had minimum mol.wts. of 52 000, 53 000 and 54 000 as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and are designated as P-450(L), P-450(M) and P-450(H) respectively. They were shown to be immunoidentical by Ouchterlony double-diffu...
متن کاملMechanism of interferon action. Characterization of sites of phosphorylation in the interferon-induced phosphoprotein P1 from mouse fibroblasts: evidence for two forms of P1.
The sites of phosphorylation of the interferon (IFN)induced protein designated Pi isolated from mouse L29 cells were characterized by partial proteolysis peptide mapping and by phosphoamino acid analysis. The Mr = 67,000 protein P1 phosphorylated in the presence of double-stranded RNA (dsRNA) was isolated from ribosomnal salt wash fractions of untreated and IFNtreated cells by poly(rI).poly(rC)...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 252 3 شماره
صفحات -
تاریخ انتشار 1977