NATURE OF THE PROTEIN CORE OF BOVINE, OVINE AND PORCINE SUBMAXILLARY MUCINS AND ITS IMPLICATIONS FOR PROTEIN SYNTHESIS**This work has been supported by a grant (AM-04619) from the National Institute for Arthritis and Metabolic Diseases, U.S. Public Health Service

Publisher Summary This chapter discusses the nature of the protein core of bovine, ovine, and porcine submaxillary mucins and describes its implications for protein synthesis. Protein biosynthesis occurs by a two-step mechanism involving the formation of small peptides at the ribosomes and their assembly by polymerases at the Golgi membrane. The existence of homologous peptides and proteins in the mucins from individual glands has important consequences for the concept of evolutionary processes. The lack of blood group activity for the inactive mucin can be expected to arise from the presence of carbohydrate chains shorter than for those for the H and A types. A limited number of synthesizing sites for peptides, containing 16 to 30 amino acids, can produce a pool of peptides from which an unlimited number of proteins can be assembled at a specific enzyme site for each protein. Specific short sequences needed for a particular function—for example, the basic chains of histones—can be separately synthesized and incorporated.