Page 40 - Anatomy and Physiology of Farm Animals, 8th Edition
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Anatomy and Physiology of the Cell / 25

               of consumption for maintenance of           (A)                       COOH
  VetBooks.ir  hydration can be severely compromised
               if an animal  is not  able to  absorb  the
               water correctly from its intestines;
               severe dehydration can occur in animals                              Leucine
               with signs of vomiting or diarrhea.
                                                                     H 2 N
               Proteins
                                                                 Lysine           Arginine
               After water, proteins are the next largest
               constituent of protoplasm.  Proteins are
               complex high‐molecular‐weight colloidal                Histidine  Phenylalanine
               molecules consisting primarily of amino
               acids that are polymerized (joined) into
               polypeptide chains (Fig.  2‐2A). Twenty
               different amino acids are specified by the   (B)
               mammalian genetic code and are combined
               to form a variety of proteins. The union of
               amino acids within a protein molecule is
               by way of a peptide linkage, a bond between
               the amino (NH ) group of one amino acid                             Chemical
                                                                                    bonds
                             2
               and the carboxyl (COOH) group of another
               amino acid, with the elimination of water.
               A small chain of amino acids is called a
               peptide. A polypeptide is a chain of more
               than 50 amino acids connected by peptide
               linkages, and a chain that contains more
               than 100 amino acids is called a protein.
               These chains of amino acids are referred to
               as the primary structure of the protein.
                  The peptide linkages between amino    Figure 2-2.  (A) A chain of amino acids joined
               acids in a protein are somewhat flexible, and   by peptide bonds to form a protein. (B) A large
               this permits the chain to bend into various   protein. Each filled circle represents a single
               three‐dimensional shapes (Fig. 2‐2B). The   amino acid. Chemical bonds between amino acids
                                                        at distant points in the chain produce the three‐
               configurations in this secondary structure   dimensional shape of the protein molecule.
               may become relatively stable, because
               chemical attractions (hydrogen bonds)
               form between amino acids at various points   proteins, and examples of each, are as
               in the chain. The final three‐dimensional   follows:
               shape, or tertiary structure, of a protein is   1.  Albumins (plasma albumin, milk
               an  important  determinant  of  its  biologic   lactalbumin)
               function, because the shape can determine   2.  Globulins (plasma globulins, globulins
               what segments of the protein chain are      in plant seeds)
               exposed and available to interact with other   3.  Protamines (in sperm cells)
               molecules.                               4.  Histones (with nucleoproteins in cell
                  Amino acids, and thus proteins, contain
                                                           nuclei)
               carbon, hydrogen, oxygen, and nitrogen.   5.  Albuminoids (collagen and elastin of
               Proteins may also contain other elements    connective tissue)
               such as sulfur, phosphorus, or iron. Simple
               proteins yield only amino acids or their    Conjugated proteins consist of simple
               derivatives upon hydrolysis. The simple   proteins combined with a component that
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