Delineations of forest fungi: Morphology and relationships of vararia

Summary Vararia belongs in a group of hymenomycetes characterized by non-xanthochroic basidiocarps in which gloeocystidia are formed rather regularly. Basidia and gloeocystidia originate at a relatively deep level in a catahymenium or hyphidial hymenium; thus they are overgrown by continuing development of the hyphal elements. As a result, they may become deeply submerged in the structure of the basidiocarp, together with embedded basidiospores. Dichohyphidia are formed as dichotomously-branched structures of limited growth. Although commonly subulate, dichohyphidia may show a considerable range of form even within a single basidiocarp. In Melzer's iodine reagent they commonly exhibit a dextrinoid reaction by becoming reddish brown. Hyphae of basidiocarps and cultures of some species have clamp-connections; those of other species lack clamps. Spores of the various species may be fusoid-ellipsoid, ellipsoid, globose, or cylindric, and may have either prominent or obscure amyloid ornamentation or may be apparently non-amyloid. Together with cultural characteristics such as the presence or absence of oedocephaloid conidiophores and various hyphal modifications, the hyphal and spore characteristics of the basidiocarp seem to present a potential basis for division ofVararia into several subgenera or generic segregates. The preceding considerations form the basis for a discussion of the position and relationships ofVararia within the Aphyllophorales.     

A rapid, two-step method for high-yield purification of recombinant rat acidic and basic fibroblast growth factors

We describe the preparation of vectors for T7 polymerase-driven, high-level expression of rat acidic (aFGF) or basic (bFGF) fibroblast growth factors in Escherichia coli. Following isopropyl-beta-D-thiogalactoside induction of T7 polymerase, rat aFGF or bFGF represented a major portion of the proteins synthesized by vector-transformed E. coli. Passage of cell extracts through an Amicon YM-100 membrane provided ultrafiltrates containing either aFGF or bFGF as the principal component. A single heparin-Sepharose chromatography of the ultrafiltrates yielded essentially homogenous, biologically active, recombinant rat aFGF or bFGF. By silanizing vessels and using buffers containing 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid, we could store homogenous aFGF or bFGF preparations without significant loss during repeated freezing and thawing. Previous methods for purifying aFGF or bFGF utilized salt fractionation followed by sequential ion exchange and heparin-Sepharose chromatography. These purified aFGF or bFGF preparations routinely were stored in buffered carrier protein to minimize mitogen loss resulting from adsorption to glass or plastic surfaces. In contrast, the methods that we detail are rapid, require minimal manipulation of preparations, and permit storage of carrier-free, homogenous preparations without loss resulting from surface adsorption. The protocols can be used for preparation of homogenous aFGF or bFGF of other species and may be readily applied to the isolation and characterization of FGF-like mitogens present in cultured cell extracts, conditioned medium, or tissue preparations.     

Synthesis and secretion of an estrus stage-specific protein by rat uterus.

A specific protein with an estimated molecular weight of 260 kDa was found to be synthesized and secreted into the incubation medium by rat uterus only during the estrus stage of the cycle. This secreted uterine protein was designated as estrus stage-specific protein (ESP). ESP was not produced by pregnant, lactating or immature pup rat uteri. Estradiol administered to ovariectomized rats induced production of ESP which was blocked by the antiestrogen, ICI 182, 780. The present results show that the synthesis and secretion of ESP is regulated by estradiol and this protein maybe involved in blastocyst implantation.