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Carboxypeptidase C acts on any C-terminal residue.
Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of the protein. Aminopeptidase M catalyzes the cleavage of all free N-terminal residues. Cleavage of disulfide bonds If protein is made up of two or more polypeptide chains and held together by noncovalent bonds then denaturing agents, such as urea or guanidine hydrochloride, are used to dissociate the chains from one another.
But polypeptide chains linked by disulfide bonds can be separated by two common methods. These methods are used to break disulfide bonds and also to prevent their reformation.
Oxidation of disulfide bonds with performic acid produces two cysteic acid residues. Because these cysteic acid side chains are ionized SO3 groups, electrostatic repulsion prevents S-S recombination.
The second method involves the reduction by -mercaptoethanol or dithiothreitol Clelands reagent to form cysteine residues. This reaction is followed by further modification of the reactive SH groups to prevent reformation of the disulfide bond.
Bioenergetics and Catalysis 3. The Cell: Structure and Function 5.
RNA synthesis and processing 8. Protein synthesis and processing 9.
Control of the gene expression Unit-IV: Host parasites interactions Cell signaling and cellular communication Cancer Unit-V: Immune system Concept and early development in plants and animals Unit-VI: Concept and early development in plants and animals Unit-VI: Morphogenesis and organogenesis in plants andanimals Physiological metabolism in plants Growth hormone and photobiology Unit-VII: Solute transport and stress physiology Digestion and respiratory system Blood vascular system Excretory system and thermoregulation Human and Quantitative Genetics Genetic Variation Unit-IX: