Homologies between paraflagellar rod proteins from trypanosomes and euglenoids revealed by a monoclonal antibody

A Nonidet P 40 insoluble fraction was isolated from Trypanosoma brucei and was used to raise a monoclonal antibody (5E9). The antigen was localized by indirect immunofluorescence in the flagellum of T. brucei and of two species of euglenoids, Euglena gracilis and Distigma proteus. In immunoblot analysis, 5E9 appeared to bind to paraflagellar rod proteins PFR1 and PFR2 of T. brucei (72000 and 75000 mol. wt.) and of E. gracilis (67000 and 76000 mol. wt.). The presence of a common epitope in paraflagellar rod proteins from species of trypanosomes and euglenoids shows that despite distinct structures of the rods some identical domain exists in the proteins that could be involved in their supramolecular assembly into a similar organelle. The antigenic determinant defined by 5E9 was also shown to be present in a 87000 molecular weight polypeptide located in the proximal part of the flagellum of Crithidia oncopelti in which a paraflagellar rod is not detectable at the ultrastructural level.     

Pectolytic clostridia isolated from sugar beet pulp silages in Italy

Twenty-eight strains of pectolytic clostridia were isolated from sugar beet pulp silages. Seventeen non-pigmented strains were presumed to be Clostridium acetobutylicum ; the remaining 11 pigmented strains were similar to Cl. felsineum. The addition of molasses to sugar beet pulps favoured the growth of other bacteria, particularly lactic acid organisms, whereas pectolytic clostridia were only occasionally found. The pectolytic clostridia promoted the structure loss of simulated silages. The use of molasses in sugar beet pulp ensiling was suggested to prevent texture loss of the ensiled mass.     

The relationship of hormone-sensitive and hormone-insensitive phosphatidylinositol to phosphatidylinositol 4,5-bisphosphate in the WRK-1 cell

We have previously characterized two distinct pools of phosphatidylinositol (PI) in the WRK-1 rat mammary tumor cell, one whose metabolism is enhanced in response to vasopressin and another which is insensitive to hormonal manipulation. The purpose of the present study was to examine the relationship between cellular phosphatidylinositol 4,5-bisphosphate (PIP2) and each of the two PI pools. We have found that in WRK-1 cells, vasopressin induces the rapid loss of PIP2 and the accumulation of inositol phosphates. By making use of kinetic differences in 32Pi uptake into the two pools of PI and assessing radioactivity levels in the 1-phosphate of PIP2, we have determined that hormone-sensitive PI is the precursor of approximately 60% of the cellular PIP2; the remainder is synthesized from the hormone-insensitive pool. Additional data indicate that PIP2 derived from hormone-sensitive PI is likewise hormone-sensitive, while that synthesized from hormone-insensitive PI remains stable over a long period of time and is not affected by the presence of vasopressin.     

THE LOCOMOTION OF LIMAX : I. TEMPERATURE COEFFICIENT OF PEDAL ACTIVITY.

Pedal progression of the slug Limax maximus was studied to obtain relations between wave velocity on the sole of the foot, wave frequency, the advance due to a single wave, and the velocity of vertically upward creeping. Each of the first three quantities is directly proportional to the simultaneous velocity of progression. Under comparable conditions, that is when work is done at a constant rate, the frequency of pedal waves is influenced by the temperature according to the equation of Arrhenius, with µ = 10,700 (Q ₁₀ for 11° to 21° = 2.1). The velocity of a single wave must have very nearly the same "temperature characteristic," which is found also in another case of nerve net transmission (in Renilla).     

Identification of the protein HC receptor

In the present study, we demonstrate for the first time the presence of a specific receptor for protein HC on the surface of human cells using the human histiocytic lymphoma cell line U937. Cells treated for 4 days with the maturation inducer phorbol 12-myristate 13-acetate, were found to increase both the number of cells binding protein HC (76% higher than for untreated cells) and the expression of protein HC receptors. Protein HC bound to these cells in a specific and saturable manner. Scatchard analysis at 4 degrees C, using radioiodinated protein HC, indicated a single class of low-affinity receptor (Ka = 2-5 x 10(7) M-1) and 20,000-30,000 receptors per cell. Monoclonal antibodies against protein HC abrogated specific binding of this protein to U937. In contrast, monoclonal antibodies that did not react with protein HC (anti-LFA-1 alpha, anti-MO1 alpha) were without effect on the binding reaction.