Abstract
Reductive methylation of the three amino groups of porcine insulin was accomplished by incubation with formaldehyde and sodium cyanoborohydride. The two amino termini and the epsilon amino group of B29 lysine were each dimethylated within 1 h of incubation. The fully methylated insulin bound more tightly to a reverse phase column than did native insulin, had a slightly more acid isoelectric point, and maintained approximately 50% biological activity when examined with an insulin sensitive cultured cell line. Reductive methylation with sodium cyanoboro (/sup 3/H) hydride resulted in a (/sup 3/H) methylated insulin with a specific activity of 6 Ci/mmol.
Marsh, J W;
Nahum, A;
Steiner, D F
[1]
- Department of Biochemistry, University of Chicago, Illinois, USA
Citation Formats
Marsh, J W, Nahum, A, and Steiner, D F.
Reductive methylation of insulin. Production of a biologically active tritiated insulin.
Denmark: N. p.,
1983.
Web.
Marsh, J W, Nahum, A, & Steiner, D F.
Reductive methylation of insulin. Production of a biologically active tritiated insulin.
Denmark.
Marsh, J W, Nahum, A, and Steiner, D F.
1983.
"Reductive methylation of insulin. Production of a biologically active tritiated insulin."
Denmark.
@misc{etde_5317000,
title = {Reductive methylation of insulin. Production of a biologically active tritiated insulin}
author = {Marsh, J W, Nahum, A, and Steiner, D F}
abstractNote = {Reductive methylation of the three amino groups of porcine insulin was accomplished by incubation with formaldehyde and sodium cyanoborohydride. The two amino termini and the epsilon amino group of B29 lysine were each dimethylated within 1 h of incubation. The fully methylated insulin bound more tightly to a reverse phase column than did native insulin, had a slightly more acid isoelectric point, and maintained approximately 50% biological activity when examined with an insulin sensitive cultured cell line. Reductive methylation with sodium cyanoboro (/sup 3/H) hydride resulted in a (/sup 3/H) methylated insulin with a specific activity of 6 Ci/mmol.}
journal = []
volume = {22}
journal type = {AC}
place = {Denmark}
year = {1983}
month = {Jan}
}
title = {Reductive methylation of insulin. Production of a biologically active tritiated insulin}
author = {Marsh, J W, Nahum, A, and Steiner, D F}
abstractNote = {Reductive methylation of the three amino groups of porcine insulin was accomplished by incubation with formaldehyde and sodium cyanoborohydride. The two amino termini and the epsilon amino group of B29 lysine were each dimethylated within 1 h of incubation. The fully methylated insulin bound more tightly to a reverse phase column than did native insulin, had a slightly more acid isoelectric point, and maintained approximately 50% biological activity when examined with an insulin sensitive cultured cell line. Reductive methylation with sodium cyanoboro (/sup 3/H) hydride resulted in a (/sup 3/H) methylated insulin with a specific activity of 6 Ci/mmol.}
journal = []
volume = {22}
journal type = {AC}
place = {Denmark}
year = {1983}
month = {Jan}
}