An unusual receptor in the octopus

The epithelium of the rim of the octopus sucker is the site of several different types of primary receptors. One is a non-ciliated cell with unusual characteristics. (1) The surface of the cell is extremely irregular with finger-like extensions of cytoplasm, especially far reaching in the basal region. (2) The slender neck contains a canal whose apical opening is in contact with the environment. This canal is lined with microvilli and contains granular material in an electron-dense matrix. (3) Patches of presumed glycogen granules occur throughout the cell, being especially abundant in the outer reaches of the cytoplasmic extensions. Their presence, together with numerous mitochondria and free ribosomes, indicate a high intrinsic metabolism. (4) Small fascicles of microtubules are randomly situated throughout the perikaryon. They gather into a coherent system of larger and larger bundles which ultimately enter the axon leading from the cell. This axon extends some distance in the basal region of the epithelium before crossing the subepithelial space to enter the infundibular muscle. Possible functions of this cell are discussed. On the basis of its specific position on the sucker and its intrinsic morphology we suggest that it is a mechanoreceptor involved in shape and/or negative pressure discrimination.     

Immunological studies of the relationship between the antigenic change of Ascaris oocytes and the junctional fluid of the fertilization chamber

Antigenic change on the surface of immature oocytes of Ascaris occurred during passage through the oviduct. Using immunodiffusion and immunoelectrophoretic techniques we examined the possible relationship between the antigenic change of immature oocytes and the junctional fluid (JF) which is present in the fertilization chamber. From the immunodiffusion it was found that the anti-immature oocyte serum (A-I serum) had more immunoprecipitation arcs than did the anti-mature oocyte serum (A-M serum) when reacted against the junctional fluid. This indicated that A-I serum contained more immunoglobulins that reacted with junctional fluid than did the A-M serum. This result was substantiated by using immunoelectrophoretic analysis and two dimension crossed immunoelectrophoresis. Our results suggest that during the migration toward the oviduct-uterine junction the immature oocytes might shed surface proteins into the luminal fluid. Alternatively, the membrane surface of mature oocytes may be altered by the interaction with the substances present in the junctional fluid.     

A spectroscopic examination on intermolecular interaction of ergosterol with lecithin

The ergosterol and lecithin absorption IR-spectra were studied in a nonpolar anhydrous medium. The thermodynamical and spectral characteristics of dimeric associates and the enthalpy value for trimeric associates of this sterol are determined. Thermodynamical and spectral parameters of ergosterol intermolecular associates with lecithin in a nonpolar anhydrous medium are found. It is established that the intermolecular interaction of lecithin with ergosterol occurs according to the mechanism of hydrogen bond. A conclusion is drawn that the presence of binary bonds and methyl groups in the cyclic and aliphatic parts of the sterol molecule affects greatly the structure of the model membrane and its strength. It is shown that under conditions of the experiment the oxygen of the phosphate group contributes to formation of the molecular associates of lecithin with sterols and not that of the carbonyl group. The obtained experimental data may be at use when studying structural disturbances of native membranes in norm and with different pathologies.     

Isolation and various characteristics of tryptophan deaminase from Proteus vulgaris

Tryptophan deaminase was isolated from Proteus vulgaris and purified. The procedure for enzyme purification included the cell destruction on USD-1, fractionation by ammonium sulphate, gel chromatography on ultragel AcA34, ion exchange chromatography on DEAE-cellulose. A degree of the enzyme purification--95, yield--5.7%. The pH optimum was 7.5, the temperature optimum--47 degrees C. The enzyme molecular weight (105 kD) was estimated by gel chromatography on Sephadex G-200, Km--5.0 mM in the K-phosphate buffer (pH 7.5). The SH groups are supposed to be present in the active site of the enzyme. The enzyme does not accelerate oxidation deamination of phenylalanine and tyrosine.