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Presents information on a study that measured plasma levels of diphenylhydantoin in an intoxicated patient and correlated with the clinical features. Methodology of the study; Results and discussion on the study.

Thymocytes from 1-month-old NZB/W mice were separated at unit gravity and then studied for helper or suppressor effects in a GVH assay. Thymocytes with a settling rate of 4 to 6 mm/hr suppressed but did not help. In contrast, help but no suppression characterized thymocytes settling at 6 to 10 mm/hr. Thus helper and suppressor thymocytes in this GVH assay were physically separated.

Two prodigiosin-like pigments from Streptomyces sp. were shown to be undecylprodiginine (i) and butylcycloheptylprodiginine (v). The antimalarial activity of five prodiginine pigments is given.

1. Permethylation and g.l.c.-mass spectrometric analysis of bile from an isolated rat liver perfusion to which methocarmol was added showed seven components not present in control bile: methocarbamol, glucuronides of methocarbamol and desmethyl-methocarbamol, and four glucuronides of hydroxylated methocarbamol metabolites. 2. An interesting rearrangement of a methyl group has been found in the mass spectrum of 3-(2-methoxyphenyloxy)-1,2-dimethoxypropane, the permethylation product from methocarbamol.

Prodigiosin, the bright red tripyrrole pigment from Serratia marcescens, has also been identified in Pseudomonas magnesiorubra, Vibrio psychroerythrus, and two Gram-negative rod-shaped mesophilic marine bacteria not members of the genus Serratia. Prodigiosin is sometimes bound to proteins; thus, extracts may require acid treatment before isolation of the pigment. Higher homologs of prodigiosin have been detected by mass spectroscopy. A mutant strain of S. marcescens produced nor-prodigiosin, in which the methoxy group of prodigiosin is replaced by a hydroxy group. Another mutant strain produced a blue tetrapyrrole pigment whose structure is a dimer of prodigiosin's rings A and B. Three novel biosynthetic analogs of prodigiosin have been obtained using a colorless mutant which does make rings A and B but not ring C and which can couple rings A and B with some added monopyrroles similar to ring C. The structures of three prodiginine (prodigiosin-like) pigments from streptomyces have been elucidated. All have the methoxytripyrrole aromatic nucleus of prodigiosin and all have an 11 carbon aliphatic side chain attached at carbon 2 of ring C. In two of the pigments the side chain is also linked to another carbon of ring C. The earlier literature about prodiginine pigments from actinomycetes has been interpreted and evaluated in light of the most recent findings. The structure elucidation of six prodiginine pigments from Actinomadurae (Nocardiae) has been completed. Only one, undecylprodiginine, is the same as from a streptomycete. For three of the six pigments, nine carbon side chains are observed and in four of them the side chain is attached to carbon 5 of ring A as well as carbon 2 of ring C so that a large ring is formed which includes the three pyrrole moieties. A section on identification summarized useful methods and presents information with which any known prodiginine pigment can be identified. The final step in the biosynthesis of prodigiosin was known to be the coupling of methoxybipyrrolecarboxaldehyde (rings A and B) with methylpentylpyrrole (ring C). Recent work using 13C-labeled precursors and Fourier transform 13C nuclear magnetic resonance has shown the pattern of incorporation for acetate, proline, glycine, serine alanine, and methionine into prodigiosin. Each pyrrole ring is constructed in a different way. Two of the streptomyces pigments have also been investigated; the pattern of incorporation is similar to that for prodigiosin. The biological activities of some prodiginine pigments are summarized. All show activity against several Gram-positive bacteria; some have anti-malarial activity. Prodigiosin has been tested clinically against coccidioidomycosis.

Red pigments were extracted from Streptoverticillium rubrireticuli strain 100-19, an organism frequently incriminated in pink staining of polyvinyl chloride. These pigments were identified as undecylprodiginine and butylcycloheptylprodiginine.

Pentobarbial, thiopental and the convulsant 5-ethyl-5-(2-cyclohexylideneëthyl) barbituric acid (CHEB) were tested for contractor effect on the isolated lung of the fullfrog at pH 7.0 (7% CO2 and 20 mM HCO3-) and pH 8.4 (0.3% CO2 and 20mM HCO3-). CHEB was a potent contractor, thiopental a feeble contractor, and pentobarbital lacked contractor effect. The contractor potencies of both CHEB and thiopental were greater at the more acid pH. The potencies of formally charged agonists such as acetylcholine and K+ were not altered by the pH differences employed in these experiments. The pKa of CHEB was found to be 8.18 at 15 degrees C and 8.03 at 27 degrees C. Calculation of concentration-effect relationships of ionized and nonionized CHEB showed that only the nonionized CHEB was responsible for the contractor effect.

The red pigment of Vibrio psychroerythrus (formerly marine psychrophile NRC 1004) was identified as prodigiosin by comparison of its mass spectrum, absorption spectrum in the visible range, and chromatographic behavior with prodigiosin isolated from Serratia marcescens. The properties of the V. psychroerythrus pigment were clearly distinguishable from five other prodigiosin-like compounds isolated from three different microorganisms.

Thirteen red strains of Actinomadura (Nocardia) pelletieri and three of A. madurae were shown to produce prodigiosin-like pigments. Both of the two major pigments which were observed on thin-layer chromatograms had R(F) values significantly greater than prodigiosin. The main pigment from A. madurae 953 was shown by mass and nuclear magnetic resonance spectroscopies to be nonylprodigiosin. The major pigment from A. pellitieri had a C(11)H(22) side chain in a ring form, but it was distinctly different from metacycloprodigiosin. "Prodiginine" was proposed as a name for the invariant aromatic portion of the prodigiosin structure.