Congenital dyserytropoietic anaemia, type II (HEMPAS) in three siblings

These siblings of a Czech family aged 21, 19 and 6 years, respectively, with congenital dyserythropoietic anemia, type II, (HEMPAS) are reported. In two elder siblings ferrokinetic studies revealed a rapid plasma 59Fe clearance, markedly decreased erythrocyte incorporation and shortened 51Cr red-cell survival. Direct anti-globulin test was found positive in one of them. Further investigations revealed low values of blood plasma cholesterol, total lipids, beta-lipoproteins, beta-carotine and vitamin E and A as well as low values of the prothrombin complex. Liver biopsy demonstrated siderosis and disseminated intravascular coagulation in the liver in both patients. The possible reasons for these humoral aberrations are discussed.     

Localization of ribosomal genes and nucleolar activity in lymphocytes of swine (Sus scrofa domestica) stimulated by phytohemagglutinins

The Pig chromosomes that contain rDNA sites displayed a polymorphism in the distribution of the genes among the nucleolar organizers located on pairs Nos. 8 and 10. Two, or more often three, active sites were observed in the chromosomes of lymphocytes stimulated with phytohemagglutinin. Only 5% of the metaphases showed a 4th small active site. At the onset of stimulation most cells contained one-two nucleoli; four nucleoli were never observed. After prolonged stimulation, the number of nuclei containing three nucleoli increased. A 4th small nucleolus appeared in a few cells, presumably formed by activation of the smallest rDNA site.     

Inhibition of protein and lipid synthesis in muscle by 2,4-dinitrofluorobenzene, an inhibitor of creatine phosphokinase

A photoaffinity label, 4-azidobenzoyltrimethionine has been synthesized. It competitively inhibits trimethionine uptake in the yeast C. albicans. Upon UV irradiation it irreversibly and specifically blocks oligopeptide uptake. These results give the first example of photoinhibition of peptide uptake in yeast.     

Structure-activity relations of the molluscan neuropeptide FMRFamide on some molluscan muscles

Analogs of the molluscan neuropeptide FMRFamide were tested on four different molluscan muscle preparations which show qualitatively different responses to the peptide; the structure-activity relations are basically similar, but not identical. The C-terminal amide and the Arg³ residue are critical for FMRFamide-like activity on all four preparations. In contrast, analogs extended at the N-terminal or with conservative substitutions for the Phe¹ or Met² residue are approximately equipotent to FMRFamide. These structural requirements parallel those for the C-terminal tetrapeptide amide of gastrin.