Please answer I will give you like Dwarfism was found to be a result of the overproduction of Enzyme X that deactivates the growth hormone. Initial fractionation using Sephadex G-100, a molecular sieve, was done, followed by subsequent purification steps until a pure form of Enzyme X was obtained. Part of the study on Enzyme X was the determination of its primary structure. Because of its big size, Enzyme X was cut into smaller peptides by treatment of enzymes and cyanogen bromide. One of the fragments was hydrolyzed and the amino acid components were separated by ion-exchange chromatography and identified. The amino acids were found to be: arg, asp, ile, lys, met, and tyr. The sequence was determined as follows: Treatment with DNFB gave a mixture of amino acids and DNP-lys Treatment with trypsin gave an amino acid, a dipeptide and a tripeptide ; the tripeptide tested positive with the Sakaguchi test Treatment with CNBr gave two tripeptides Treatment with chymotrypsin gave a dipeptide and a tetrapeptide; the dipeptide tested positive with the Xanthoproteic test Treatment with streptococcal protease gave an amino acid and a pentapeptide 2.1. What is the amino acid sequence of the peptide? 2.2. What is the pI of the peptide?

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Please answer I will give you like Dwarfism was found to be a result of the overproduction of Enzyme X that deactivates the growth hormone. Initial fractionation using Sephadex G-100, a molecular sieve, was done, followed by subsequent purification steps until a pure form of Enzyme X was obtained. Part of the study on Enzyme X was the determination of its primary structure. Because of its big size, Enzyme X was cut into smaller peptides by treatment of enzymes and cyanogen bromide. One of the fragments was hydrolyzed and the amino acid components were separated by ion-exchange chromatography and identified. The amino acids were found to be: arg, asp, ile, lys, met, and tyr. The sequence was determined as follows: Treatment with DNFB gave a mixture of amino acids and DNP-lys Treatment with trypsin gave an amino acid, a dipeptide and a tripeptide ; the tripeptide tested positive with the Sakaguchi test Treatment with CNBr gave two tripeptides Treatment with chymotrypsin gave a dipeptide and a tetrapeptide; the dipeptide tested positive with the Xanthoproteic test Treatment with streptococcal protease gave an amino acid and a pentapeptide 2.1. What is the amino acid sequence of the peptide? 2.2. What is the pI of the peptide?

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