Semisynthesis of Human Insulin Utilizing Chemically Modified Carboxypeptidase

نویسنده

  • K. BREDDAM
چکیده

It has previously been demonstrated that the C-terminal alanyl residue in the B-chain of porcine insulin can be exchanged with a threonyl residue in a carboxypeptidase Y catalyzed transpeptidation reaction using threonine amide as nucleophile. However, with this procedure the transpeptidation product, human insulin amide, was obtained in relatively low yields. In the present paper it is demonstrated that mercury halide derivatives of CPD-Y catalyze the transpeptidation reaction with porcine insulin effectively and human insulin amide could be isolated in high yield. It is also demonstrated that deamidation of human insulin amide to yield essentially homogeneous human insulin can be achieved using CPD-Y modified with methyl mercuric iodide (Me-Hg-CPD-Y).

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The modified recombinant proinsulin: a simple and efficient route to produce insulin glargine in E. coli

Background: Recombinant insulin glargine, a long-acting analogue of insulin, is expressed as proinsulin in host cell and after purification and refolding steps cleaved to active insulin by enzymatic digestion using trypsin and carboxypeptidase B. Since the proinsulin's B and C chains have several internal arginine and lysine residues, a number of impurities are generated following treatment wit...

متن کامل

CHEMICALLY MODIFIED CARBOXYPEPTIDASE Y WITH INCREASED AMIDASE ACTIVITY by

Treatment of carboxypeptidase Y with ~4C-iodoacetamide caused a drastic reduction in the peptidase activity towards FA-Phe-$Leu-OH while the esterase activity towards FA-Phe 89 the amidase activity towards FA-PhelNH2 and the peptidyl amino acid amide hydrolase activity towards FA-Phe-$GIy-NH2 were much less affected. The loss of peptidase activity could be correlated with the incorporation of a...

متن کامل

Carboxypeptidase Y Catalyzed C-terminal Modification in the B-chain of Porcine Insulin

It is demonstrated that carboxypeptidase Y can be used to exchange the C-terminal alanyl residue of porcine insulin with a threonyl residue, thus forming human insulin. Using threonine amide as nucleophile, the reaction proceeds as a transpeptidation via human insulin amide, des(Ala)a30(Thr-NH2)a30insulin. However, since the amidase activity of carboxypeptidase Y towards this particular insulin...

متن کامل

Electrochemical Detection of Insulin in Blood serum using Ppy/GF Nanocomposite Modified Pencil Graphite Electrode

In this study, pencil graphite electrode was modified using conductive polypyrrole (Ppy) and grapheme (GF) nanocomposite for electrochemical determination of insulin. Electrochemical behavior of insulin on PGE was investigated using cyclic voltammetric (CV) and differential pulse voltammetric (DPV) and chronoaprometry (CA) methods. Several effective parameters including pH, concentration, and s...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2008