title: Properties of Barley Seed Chitinases and Release of Embryo-Associated Isoforms during Early Stages of Imbibition.
abstract: Barley (Hordeum vulgare L.) seeds contain at least five proteins with chitinase (CH) activity. Two of these (CH1 and CH2) are found primarily in the aleurone and endosperm tissues, and the other three (CH3, CH4, and CH5) are enriched in the embryo. From the bran fraction, three of these CHs (CH1, CH2, and CH3) were purified to apparent homogeneity. These three CHs have apparent molecular masses of 27, 34, and 35 kilodaltons and isoelectric points of 9.3, 9.2, and 8.7, respectively. CH2 and CH3 have amino terminal sequences resembling a portion of the chitin-binding domain of lectins and other plant defense proteins. CH1 lacks this domain. All three CHs exhibit antifungal activity and inhibit the mycelial growth of some species of trichoderma and Fusarium in vitro. During the early period of imbibition by seeds, two of the embryo-associated CHs are selectively released into the surrounding aqueous medium.
authors: Department of Biochemistry, Willard Hall, Kansas State University, Manhattan, Kansas 66506.
authors: M
authors: M
authors: Swegle
authors: K J
authors: KJ
authors: Kramer
authors: S
authors: S
authors: Muthukrishnan