Earthworms produce a collagen-like substance detected by the garter snake vomeronasal system.

Earthworms (Lumbricus terrestris) produce a chemical substance that is readily detected by and serves as an attractant for garter snakes (Thamnophis sirtalis). This chemoattractant is sensed by the vomeronasal system of snakes. Amino acid analysis of the chemoattractant revealed a high hydroxyproline/proline ratio and large amounts of serine and threonine. More than one-third of the residues were glycine. No hydroxylysine and no cysteine were present. Carbohydrate analyses revealed a high content of galactose (11% by weight) and smaller amounts of fucose, mannose, glucose, N-acetylglucosamine, and N-acetylgalactosamine. These results were very similar to results reported for the amino acid composition and carbohydrate content of earthworm cuticle collagen and gelatin. A preparation of purified earthworm cuticle collagen proved to be a potent source of chemoattractant for garter snakes. Further, it was not possible to prepare chemoattractant from decuticlized earthworms. These results strongly suggest that a component of the earthworm chemoattractant for snakes is structurally related to earthworm cuticle collagen.

Molar absorptivity and A1%1cm values for proteins at selected wavelengths of the visible and ultraviolet regions. XXIV.

The molar absorptivity and A1%1cm values for 154 proteins are reported. The conditions under which these values were obtained and citations to the sources of the data are also provided.

Chemo-attractant for the garter snake: characterization of vomeronasally-mediated response-eliciting components of earthworm wash--III.

Heating a 0.1 N HCl solution of lyophilized garter snake, Thamnophis sirtalis, chemoattractant obtained from earthworm, Lumbricus terrestris, surface washings, in a boiling water bath, and separation by gel chromatography, gave two fractions, F2, of high molecular weight and containing all the chemoattractant activity, and F4, of low molecular weight. The activity is lost between 15 and 30 min of heating. A similarly treated 0.1 N NaOH solution of lyophilized washings gave no F2 fraction and an F4 fraction in increasing amount. All the chemoattractant activity is lost between 0 and 15 min. Separations were monitored by assays for protein and carbohydrate.

Characterization of vomeronasally-mediated response-eliciting components of earthworm wash-II.

Garter snakes reliably spend more time and tongue flick more frequently at a dish containing surface washings of earthworm (EW) than at a control dish containing water or sodium chloride. In a series of experiments EW was examined to further characterize and purify the snake-attracting component(s). Earthworm wash boiled for up to two hours did not lose its snake-attracting activity, but EW boiled for four hours was not discriminated from a control substance. The active components of EW were completely precipitated by 90 and 100% saturated ammonium sulfate solutions. The molecular weight of the active components, as determined by dialysis, is larger than 67,000 daltons. Earthworm wash was separated into two peaks on either G-75 or AcA 44. The larger peak (F2) contains snake-attracting material of molecular weight greater than 67K. The smaller peak material (F4) is inactive as a snake-attractant and contains material of approximate molecular weight of 3K. Biological activity of EW covaried with Lowry (protein) assay and Dubois (carbohydrate) assay values and 280 nm absorbance. The response eliciting components of EW are not extractable from earthworms at temperatures below 60 degrees C, but can be extracted at 60 degrees C (for one minute) from the worms or the soil that forms the bedding for the earthworms.

A compilation of amino acid analyses of proteins. XIX. Residues per thousand residues--6.

The amino acid analyses of 186 proteins are given as residues per 1000 residues. Additional information as carbohydrate composition, content of uncommon amino acids, and sources of all proteins are also presented.

Glycosylation of proteins: its implications in diabetic control and complications.

The author shows that nonenzymic glucosylation of proteins can modify the structure and function of proteins isolated from non-insulin-dependent tissues and that these glucosylated proteins, whose normal functions have been altered or removed, may be related to diabetes and some of its sequelae.

Molar absorptivity and A 1% 1cm values for proteins at selected wavelengths of the visible and ultraviolet regions. XXIII.

The molar absorptivity and A 1% 1cm values for 150 proteins are reported. The conditions under which these values were obtained and to the sources of the data are also provided.

A compilation of amino acid analyses of proteins. XVIII. Residues per thousand residues--5.

The amino acid analyses of 213 proteins, as residues per 1000 residues, are given. In addition, the carbohydrate content, the content of any noncommon amino acids, the sources of all proteins, and the necessary literature citations are given.

Preliminary characterization of response-eliciting components of earthworm extract.

Fifteen garter snakes (Thamnophis sirtalis) reliably spent more time and tongue flicked more frequently at a dish containing earthworm extract than a dish containing distilled water when these were presented simultaneously for two minute intervals. The discriminability of the earthworm extract was directly related to its concentration. Garter snakes with their vomeronasal ducts sutured closed did not respond differentially to earthworm extract and water under these test conditions. Thus their ability to discriminate earthworm extract from water in this bioassay was dependent upon a functional vomeronasal system. Earthworm extract retains its biological activity after boiling at 100 degrees C for 15 minutes and after lyophilization. Its effectiveness is not altered by changes in pH. Snakes continued to respond differentially to extracts with pH 2, 5-6 or 11. Chloroform extractions of the acid, neutral and alkaline earthworm extract yielded activity primarily in the water layer. The small amount of activity in the chloroform layer was removed by use of a drying agent. Bradford dye-binding tests indicated the presence of protein in the active fractions.

Molar absorptivity and A1 cm (1%) values for proteins at selected wavelengths of the ultraviolet and visible regions. XXII.

The molar absorptivity and A1 cm (1%) values for 150 proteins are reported. The conditions under which these values were obtained and citations to the sources of the data are also provided.