The fragments that will be produced when Bradykinin is treated with trypsin and chymotrypsin need to be identified. Concept introduction: Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin. Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine. Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

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Chapter 25, Problem 71PP

(a)

Interpretation Introduction

Interpretation:

The fragments that will be produced when Bradykinin is treated with trypsin and chymotrypsin need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

(b)

Interpretation Introduction

Interpretation:

The fragments that will be produced when Bradykinin is treated with trypsin and chymotrypsin need to be identified.

Concept introduction:

Enzymatic cleavage is a useful method for identifying the sequence of amino acid residue in a large peptide. This method uses enzymes for hydrolysis of the peptide bonds. These enzymes are known as peptidases. Some of the frequently used enzyme is trypsin and chymotrypsin.

Trypsin selectively hydrolyzes the peptide bond at the carboxyl side of arginine and lysine.

Chymotrypsin selectively hydrolyzes the peptide bond at the carboxyl end of amino acids containing aromatic side chains. The amino acids which have aromatic side chains are phenylalanine, tyrosine and tryptophan.

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