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PubMed1986

[Isolation and partial characterization of allergen from Bermuda grass pollen].

Allergens of bermuda grass pollen extract have been studied and identified. Immunoblotting studies revealed that at least 12 SDS-denatured polypeptide showed IgE-binding activity. Molecular weight was estimated between 10,000 to 90,000 daltons. An allergenic component was isolated by a combination of ion exchange chromatography and gel filtration chromatography. The allergen preparation was shown to be homogeneous by PAGE and SDS-PAGE studies. Allergen was found to be an acidic protein with a molecular size of the order of 16,300 daltons. Ultraviolet spectrum scanning showed weak absorption at 280 nm. Amino acid analysis revealed that the purified allergen contained no tyrosine, proline and cysteine residues but contained a high percentage of glutamic acid and aspartic acid residues. The results of amino analysis indicate that tyrosine, proline and cysteine residues are not involved in the allergenic determinant site.

Allergens↗
PubMed1995

Oviposition responses of Culex tarsalis and Culex quinquefasciatus to aged Bermuda grass infusions.

Fermented infusions of organic matter are commonly used as baits in traps for gravid female mosquitoes. However, infusions are dynamic, and their effects on mosquito oviposition as their chemical and microbial constituents change over time are not well documented. Bermuda grass infusion fermented for periods of 0-63 days was stimulatory to gravid Culex quinquefasciatus. In contrast, only 5-25-day-old infusion was stimulatory to Culex tarsalis. Standard-aged infusion (7 days old) was as effective or better than infusion of any other age for Cx. tarsalis, whereas Cx. quinquefasciatus exhibited a distinct preference for 2-4-wk-old infusion. The results are discussed in terms of mosquito species' oviposition site preferences and in terms of mosquito surveillance programs.

Animals↗
PubMed1977

Studies on Bermuda grass pollen allergens.

Two allergens, BGP-1 and BGP-2, were identified in crude Bermuda grass pollen extract. BGP-1 was a major allergen and elicited a skin reaction in all subjects sensitive to the crude extract, whereas BGP-2 was a minor allergen and elicited a reaction in only 75% of such subjects. Calibrated column chromatography was used to determine the molecular weights and Stokes radii of the allergens. For BGP-1 they were 30 000 daltons and 24,3 X 10(-8) cm respectively and for BGP-2 they were 14 000 daltons and 18,1 X 10(-8) respectively. The sedimentation coefficient (S20,w) of BGP-1 on sucrose density gradient ultracentrifugation was 3,1 and on iso-electric focusing its iso-electric point was found to be pH 5,4. The reason why only certain individuals sensitive to BGP-1 are sensitive to BGP-2 is discussed. It is possible that the former is a dimer of the latter.

Centrifugation, Density Gradient↗
PubMed1997

Molecular characterization of four members of the alpha-tubulin gene family of the Bermuda land crab Gecarcinus lateralis.

Four alpha-tubulin isoforms recovered from a cDNA library from regenerating limb buds of the Bermuda land crab Gecarcinus lateralis have been characterized. Two clones (alpha 1 and alpha 2) contained complete coding sequences with start and stop codons; the other two clones were partial, lacking 5' ends. The four isoforms showed high homology in their coding sequences but rather low homology in their non-coding regions. Identity between the nucleotide sequences of alpha 1 and alpha 2 was 83.4%; between their predicted amino acid sequences it was 88.9%. The inferred number of amino acid residues for both alpha 1 and alpha 2 was 451, and their calculated molecular weights were 58.29 and 58.45 kDa, respectively. The greatest divergence in the predicted crab alpha-tubulin proteins occurred near the carboxy terminus, as in alpha-tubulins of other organisms. When compared with other species; nucleotide sequences of all four clones showed highest homology to alpha-tubulin genes of an insect (Drosophila melanogaster), while their predicted amino acid sequences were most highly homologous to an alpha-tubulin of a mammal (Rattus norvegicus). Southern blots revealed a total of five to seven alpha-tubulin genes encoded in the G. lateralis genome. Northern blots showed single bands of approximately 2.2 kb with an alpha 1-tubulin probe and 1.9 kb with an alpha 2-tubulin probe. mRNA levels of both tubulin isoforms appeared to be independently regulated at different stages of the intermolt cycle in both epidermis and limb buds. Western blots of 1D gels of proteins from epidermis, limb buds, or claw muscle showed tissue- and stage-specific changes in tubulin content; similar analyses on blots of 2D gels revealed differences in the number of alpha-tubulin isoforms that were expressed.

Amino Acid Sequence↗
PubMed1985

Bermuda.

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Americas↗
PubMed1996

Actin-encoding cDNAs and gene expression during the intermolt cycle of the Bermuda land crab Gecarcinus lateralis.

Two actin-encoding cDNAs (act1 and act2) from Gecarcinus lateralis have been sequenced or partially sequenced and the corresponding proteins deduced. The act1 cDNA has a complete ORF; the act2 cDNA lacks most of the 5' end of the coding region. The nucleotide (nt) sequences of both clones are very similar to act sequences of many organisms, the most closely related being from another arthropod, the silkmoth Bombyx mori. The proteins Act1 and Act2 are more similar to vertebrate cytoplasmic actin isoforms (beta-actins) than to vertebrate muscle actins (alpha-actins); they are also more similar to animal actins than to those of fungi or plants. Codon usage is strongly biased toward C or G in the third position. The deduced number of amino acid (aa) residues and calculated Mr for Act1 are 376 aa and 41.94 kDa, respectively. The deduced aa sequence of Act1 is very similar to those of muscle actins of B. mori and Drosophila melanogaster. Southern blots indicated seven to eleven act genes in the crab genome. Northern blots probed with a segment from the 3' UTR of act1 showed a single band of approx. 1.6 kb in poly(A)+ mRNAs from epidermis, limb bud or claw muscle and in total RNAs from ovary and gill, and two bands of approx. 1.6 and 1.8 kb in total RNA from midgut gland. Western blots of one-dimensional gels of proteins from the four layers of the exoskeleton, epidermis, limb buds and claw muscle were probed with a monoclonal Ab against chicken gizzard actin; tissue- and stage-specific changes in actin content were observed. The presence of several isoforms, and differences in their number and occurrence at various stages of the intermolt cycle, were detected on Western blots of two-dimensional gels.

Actins↗