Alpha-keratin keratin cell due to their effect on the various hydrogen bonds in the alpha-keratin network. Alpha-keratins proteins can be one of two types: type I or type II. There are 54 keratin genes in humans, 28 of which code for type I, and 26 for type II. Type I proteins are acidic, meaning they contain more acidic amino acids, such as aspartic acid, while type II proteins are basic, meaning they contain more basic amino acids, such as lysine. This differentiation is especially important in alpha-keratins because in the synthesis of its sub-unit dimer, the coiled coil, one protein coil
Lectin their particular high specificity for foreign glycoconjugates (e.g. those of fungi, invertebrates, and animals) and used in biomedicine for blood cell testing and in biochemistry for fractionation. Although they were first discovered more than 100 years ago in plants, now lectins are known to be present throughout nature. It is generally believed that the earliest description of a lectin was given by Peter Hermann Stillmark in his doctoral thesis presented in 1888 to the University of Dorpat. Stillmark isolated ricin, an extremely toxic hemagglutinin, from seeds of the castor plant ("Ricinus communis"). The first lectin to be purified on a