o Treatment with DNFB gave a mixture of amino acids and DNP-lys o Treatment with trypsin gave an amino acid, a dipeptide and a tripeptide; the tripeptide tested positive with the Sakaguchi test o Treatment with CNBR gave two tripeptides o Treatment with chymotrypsin gave a dipeptide and a tetrapeptide; the dipeptide tested positive with the Xanthoproteic test o Treatment with streptococcal prstease gave an amino acid and a pentapeptide 2.1. What is the amino acid sequence of the peptide?

Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter4: Cells
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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:
o Treatment
ONFB gave a mixture of amino acids and DNP-lys
o Treatment with trypsin gave an amino acid, a dipeptide and a tripeptide ; the
tripeptide tested positive with the Sakaguchi test
o Treatment with CNBR gave two tripeptides
o Treatment with chymotrypsin gave a dipeptide and a tetrapeptide; the dipeptide
tested positive with the Xanthoproteic test
o Treatment with streptococcal prstease gave an amino acid and a pentapeptide
2.1. What is the amino acid sequence of the peptide?
2.2. What is the pl of the peptide?
Transcribed Image Text: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: o Treatment ONFB gave a mixture of amino acids and DNP-lys o Treatment with trypsin gave an amino acid, a dipeptide and a tripeptide ; the tripeptide tested positive with the Sakaguchi test o Treatment with CNBR gave two tripeptides o Treatment with chymotrypsin gave a dipeptide and a tetrapeptide; the dipeptide tested positive with the Xanthoproteic test o Treatment with streptococcal prstease gave an amino acid and a pentapeptide 2.1. What is the amino acid sequence of the peptide? 2.2. What is the pl of the peptide?
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