Skeletal growth in a medieval population from Sudanese Nubia

Long bone growth is analyzed for 180 children from a Medieval population at Kulubnarti in Sudanese Nubia (550–1450 A.D.). A regional interpopulation comparison is made with growth data from Wadi Halfa in Lower Nubia, and an intrapopulation analysis is undertaken to assess diachronic changes in growth at Kulubnarti. Changes in growth patterns are interpreted in the context of mortality and morbidity profiles and relationships between the three variables are discussed. It is suggested that changes in the sociopolitical environment may have been responsible in part for altering levels of biological stress and impacting growth.     

Solubilization of phospholipids by detergents. Structural and kinetic aspects

Most amphiphiles in biological membranes including phospholipids, steroids, and membrane proteins are insoluble amphiphiles and would form liquid crystals or insoluble precipitates alone in aqueous media. Detergents are soluble amphiphiles and above a critical concentration and temperature form micelles of various sizes and shapes. Much of the recent progress in studying the insoluble amphiphiles is due to the formation of thermodynamically stable isotropic solutions of these compounds in the presence of detergents. This process, which is commonly denoted as "solubilization,' involves transformation of lamellar structures into mixed micelles. The information available to date on the solubilization of phospholipids, which constitute the lipid skeleton of biomembranes, by the common detergents is discussed in this review, both with respect to the kinetics of this process and the structure of the various phospholipid-detergent mixed micelles formed. It is hoped that this discussion will lead to somewhat more useful, although still necessarily fairly empirical, approaches to the solubilization of phospholipids by detergents.     

Kinetics of dissociation of reduced nicotinamide adenine dinucleotide phosphate from its complexes with malic enzyme in relation to substrate inhibition and half-of-the-sites reactivity

Malic enzyme of pigeon liver binds NADPH at four equivalent enzyme sites and binds Mn2+ and malate each at two sets of "tight" and "weak" sites with negative cooperativity [Pry, T. A., & Hsu, R. Y. (1980) Biochemistry 19, 951-962]. Stopped-flow studies on the displacement of NADPH from the malate-enzyme complexes E4-NADPH4, E4-Mn2(2+)-NADPH4, E4-Mn2(2+)-NADPH4-dimalate, and E4-Mn2(2+)-NADPH4-tetramalate by large excess NADP+ or its analogue phosphoadenosine(2')diphospho(5')ribose show that NADPH dissociates from the binary complex rapidly with a first-order rate constant of 427 s-1. Dissociation from the ternary E4-Mn2(2+)-NADPH4 complex containing two tightly bound Mn2+ ions can be described by a single first-order process with a rate constant of 135 s-1, or more satisfactorily by two simultaneous first-order processes attributable to the reactions of Mn2+-deficient (k congruent to 427 s-1) and Mn2+-liganded (k = 96 s-1) subunits. The latter equals twice the maximum steady-state turnover rate of 53.2 + 3.0 s-1 assigned to dissociation of the reduced nucleotide from transient E-Mn2+-NADPH, and this 2:1 ratio strongly supports our proposed "half-of-the-sites" model [Hsu, R. Y., & Pry, T. A. (1980) Biochemistry 19, 962-968]. Dissociation from the E4-Mn2(2+)-NADPH4-dimalate complex (k = 100 s-1) follows only the slower process, suggesting that occupancy of malate at two sites tightens enzyme-bound NADPH on the adjacent sites. Binding of malate at two additional weak sites yields E4-Mn2(2+)-NADPH4-tetramalate and a NADPH dissociation rate constant of 2.69 s-1. The 97% decrease in NADPH dissociation parallels the observed 93% maximal inhibition by malate and is the cause of substrate inhibition.(ABSTRACT TRUNCATED AT 250 WORDS)     

Dinitrophenyl-pepstatins as active-site-directed localization reagents for cathepsin D

1. N-Pepstatinyl-N'-dinitrophenyl-1,6-diaminohexane, a potential active-site-directed localization reagent for cathepsin D, was found to bind non-specifically to immuno-precipitates containing cathepsin D. 2. Three new water-soluble localization reagents were synthesized, by using NN'-bis-(3-aminopropyl)piperazine, 3-oxa-1,5-diamino-pentane or 3,6-dioxa-1,8-diamino-octane, as spacer arms between the pepstatin and dinitrophenyl moieties. 3. The hydrophilic dinitrophenyl-pepstatins were all tight-binding inhibitors of cathepsin D at pH 3.5, but showed little or no binding to immuno-precipitates containing the inactive enzyme at pH 7.4. 4. Gel-chromatographic experiments showed that, at pH 5.0, all the dinitrophenyl-pepstatins were bifunctional reagents able to bind cathepsin D and anti-dinitrophenyl antibody at the same time. Enzyme-inhibitor-antibody complexes were not formed at pH 7.4, thus confirming that the reagents were active-site-directed. 5. Cultured human synovial cells were fixed and incubated with the dinitrophenyl-pepstatins at pH 5.0 or pH 7.4. After washing briefly, the cells were incubated at the appropriate pH value with anti-dinitrophenyl antibody labelled with fluorescein. When examined by fluorescence microscopy the cells stained at pH 5.0 showed fluorescent perinuclear granules, which were not seen in the cells treated at pH 7.4. The distribution of cathepsin D, determined by indirect immuno-fluorescence at pH 7.4, closely resembled that revealed by the dinitrophenyl-pepstatins at pH 5.0. 7. NN'-(3-Pepstatinylaminopropyl-3'-dinitrophenylaminopropyl)piperazine gave the most intense lysosomal staining and showed no non-specific binding. We conclude that this reagent is suitable for the subcellular localization of the active conformation of cathepsin D.     

Repair Kinetics of Radiation-Induced Mitotic Delay

The recovery from radiation-induced mitotic delay in asynchronous sarcoma-180 (S-180) ascites tumor cells has been analyzed in a manner analogous to the repair of sublethal damage. 200-R increments were separated by various fraction intervals (not exceeding the time necessary for mitosis to return to control levels) for total exposures up to 1600 R. The accumulated mitotic delay after the last exposure increment, in percent of an equivalent single exposure, decreased exponentially with overall treatment time in a bimodal fashion. An initial repair process displayed a half time of 2.3 h of overall elapsed time and was followed by a slower process with a half time of 15.1 h. Such a bimodal recovery provides an explanation of why fractionation intervals long with respect to the amitotic period resulting from a single 200 R exposure enhance mitotic delay over that of equivalent single exposures, while shorter fractionation intervals diminish it. It also predicts that mitotic delay vs. dose curves should bend toward the abscissa as the exposure time is increased with large single exposures and large fractionated exposures given over short fraction intervals.     

Nitrogen and phosphorus release from decaying water milfoil

To evaluate the net N and P contribution to water from herbicide-killed aquatic weeds, water milfoil containing 1.5% N and 0.30% P was killed with endothal and allowed to decompose, in the dark, in water only or sediment-water systems. Changes with time in dry weight, total N and P, and organic C in the plant material, and organic and inorganic forms of N and P in the water were determined. Plant decompostion was limited by N. Inorganic N was released by the sediment, and decomposition was more rapid when sediment was present. A smaller N requirement for decomposition under conditions of low O₂ was postulated as a possible explanation of the more rapid decomposition observed in the absence of aeration. The presence of plant P in excess of decomposition requirements resulted in rapid accumulation of organic P, followed by inorganic P, in the water. Organic N appeared in the water early in the experiments, but was depleted rapidly, and inorganic N was apparently immobilized as soon as it was formed. In the presence of sediment, organic N and inorganic P levels were much lower. On treating of water milfoil with herbicide, rapid P release can be expected. This P can either be utilized in further biomass production or be sorbed by the sediment. Insufficient data were available to reach definite conclusions regarding N. It would appear, however, that N release from decaying weeds is much slower than P.     

Ultrastructural observations on the kinetosomes,and Golgi bodies during the asexual life cycle ofSaprolegnia

Summary At the onset of zoospore cleavage the centrioles ofSaprolegnia ferax reorientate, develop into kinetosomes and become associated with microtubular roots and a striate fibre. After cytoplasmic cleavage a flagellum, with a hitherto undescribed transition zone structure, develops from each kinetosome. Flagellum axonemes occur inside recently encysted primary spores. In vegetative hyphae and germinating cysts most recognizable Golgi bodies are characteristically associated with a cisternum of the endoplasmic reticulum and a mitochondrion but during sporogenesis they all lie adjacent to nuclei where they are apparently active in vesicle production. The structural details of these changes are described and their significance discussed. We wish to acknowledge the numerous helpful discussions with Dr. J. L. Gay. The senior author held a S.R.C. studentship during the course of this work, part of which was submitted in partial fulfillment of the requirements for the degree of Ph. D. at the University of London.