[Effect of adenosine triphosphate on the cleavage of H1 histones in nuclei of rat spleen and liver]. / Vliianie adenozintrifosfata na rasshcheplenie gistonov H1 iader selezenki i pecheni krys.

Proteolysis of histones H1b and H1(0) is observed after the incubation of rat spleen nuclei at 37 degrees C during 1 hour. Adenosine triphosphate, inorganic pyrophosphate and nicotinamide adenine dinucleotide decrease the digestion of histone H1b. ATP, PP1 and NAD+, in the case of 3 hours incubation, do not affect proteolysis of H1 histones in rat spleen nuclei. The incubation of rat liver nuclei at 37 degrees C during 1 hour leads to a decrease of the amount of histone H1b and, to much more extent, H1a. In this case ATP, PP1 and NAD+ increase proteolysis of histone H1a but practically do not affect proteolysis of H1b. After 2-hours incubations histone H1a is completely digested but histone H1b is partially preserved: ATP in this case, as well as in spleen nuclei, decreases proteolysis of histone H1b. During the 3 hours incubation, when histones H H1a and H1b are completely digested, partial digestion of histone H3 being observed, ATP does not prevent from proteolysis of histone H1b. A protein appears between the H2A and H4 histones after heating at 37 degrees C in both spleen and liver rat nuclei. Neither ATP nor PP1 and NAD+ affect the amount of this protein. It is suggested that the location of histones H1a and H1b in different chromatin domains determines the digestion of these histones by ATP-dependent proteinases.

Biosynthesis and physiological role of homarine in marine shrimp.

Glycine, which contributes 2 carbon atoms and the nitrogen for the biosynthesis of homarine by homogenates of shrimp muscle, reacts metabolically with succinyl coenzyme A to form N-succinylglycine. The latter product is effectively converted by such homogenates to homarine, and it is concluded that N-succinylglycine is on the main pathway of this biosynthetic series of reactions and provides all of the required atoms in homarine, except for the N-methyl carbon. A possible pathway for the complete biosynthesis of homarine is described. Evidence is presented that homarine acts as a transmethylating agent in shrimp muscle homogenates and is capable of transferring its N-methyl group to form mono-, di-, and trimethylamines, trimethylamine oxide, choline, and betaine. In this process, homarine loses its methyl groups to form picolinic acid, and, conversely, picolinic acid can be methylated to yield homarine. It is speculated that homarine is not only a "methyl" donor but may serve as a reservoir of methyl groups in crustacea.

Biosynthesis in vitro of homarine and pyridine carboxylic acids in marine shrimp.

Minces and homogenates of muscle obtained from the marine shrimp Penaeus duorarum are capable of synthesizing homarine from [14C]glycine. Glycine carbon atoms are incorporated into homarine but not significantly into picolinate or quinolinate. [2-14C]Acetate is readily incorporated into quinolinate in the in vitro system but only slightly into homarine and not at all into picolinate. Quinolinic acid is rapidly methylated to N-methyl quinolinate which is not decarboxylated to form homarine. Procedures have been developed for the satisfactory separation of N-methyl quinolinate from homarine.

Experiments in marine biochemistry. Homarine metabolism in Penaeus duorarum.

A fractionation procedure has been developed which permits the isolation of 1 to 2 mg of homarine from a single shrimp. This procedure was used to show that homarine is endogenously synthesized by Penaeus duorarum in the free unbound form, and to study the metabolic precursors involved. Injected DL-[14C]tryptophan was not converted to [14C]homarine. However, [6-14C]quinolinic acid, a known catabolite of tryptophan, is an effective precursor. [2-14C]Acetate and [U-14C]glycerol are effectively converted to [14C]homarine while [14C]bicarbonate is poorly utilized. The injection of L-[U-14C]aspartate resulted in labeled homarine, but the quantity converted was less than expected. Since [14C]glycerol is an effective precursor there is a possibility that quinolinic acid may be formed in P. duorarum by a condensation similar to that of glyceraldehyde 3-phosphate with aspartic acid or a closely related metabolite. It is suggested that decarboxylation of quinolinic acid gives rise to picolinic acid which is methylated to yield homarine. L-[methyl-14C]Methionine efficiently provides the N-methyl carbon presumably via S-adenosylmethionine.

Chemoreception in Nassarius obsoletus: the role of specific stimulatory proteins.

Proteins in human plasma and oyster fluid induce a strong feeding response in the marine snail Nassarius obsoletus. Purified human serum albumin induces a 50 percent positive response at concentrations of 1 to 2 x 10(-9) molar. Adsorbed fatty acids markedly decrease the effectiveness of albumin. From oyster fluid a major glycoprotein has been isolated which accounts for essentially the entire stimulatory activity of the fluid and is effective at concentrations of approximately 1 to 2 x 10(-10) molar. These findings provide evidence that specific proteins in extremely low concentrations may play a major role in chemoreception in aquatic animals.