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Biomedical subjects

H Weintraub

Publications and source records attributed to H Weintraub.

At least 163 records · Page 9Linked to original sources
PubMed1976

Laboratory experience with a new autotransfusion device.

A new device for collecting and administering blood by intraoperative autotransfusion consists of several novel features: a collection bag that is kept expanded by a vacuum and into which the blood is drawn by suction of a lesser degree than the outside vacuum, a crease in the collection bag that decreases turbulence and foaming, and separation of the infusion element from the retrieval system by a valve that allows pressure infusion and suction continously. The apparatus is inexpensive, quickly assembled, operated by wall suction or suction pump. We have had favorable experience with its use in animals.

Animals↗
PubMed1976

A model for chromatin based upon two symmetrically paired half-nucleosomes.

We propose that the basic unit of chromatin is constructed of two isologously paired heterotypic protein tetramers each containing one molecule of H2A, H2B, H3, and H4 histone. These proteins form a core that holds 140 base pairs (bp) of DNA in a single left-handed, non-interwound DNA super-coil approximately 95 bp in circumference, creating a nucleosome particle (DNA and protein) organized about a dyad axis of symmetry. Such a nucleosome can open up into its separate half-nucleosomes to allow genetic readout without requiring histone displacement.

Chromatin↗
PubMed1976

Cooperative alignment of nu bodies during chromosome replication in the presence of cycloheximide.

50% of control DNA is resistant to staphylococcal nuclease after digestion in isolated nuclei, while only 25% of the labeled DNA made in the presence of cycloheximide is resistant to nuclease. Nevertheless, cycloheximide DNA is folded into normal chromosomal subunits as evidence by the observation that it generates nuclease limit-digest DNA fragments that are indistinguishable from controls. These results indicate that cycloheximide chromatin is associated with half the number of normal nu bodies. These nu bodies are probably recycled from the parental chromosome. Partial nuclease digestion of cycloheximide chromatin reveals that a normal pattern of monomer and multimer DNA fragments is generated up to octamers. The data are consistent with the idea that in the presence of cycloheximide, recycled parental histones become cooperatively aligned along the daughter double helices.

Chromatin↗
PubMed1976

Changes in anticoagulation in dogs assayed by three methods.

As a preliminary to a membrane oxygenator study, a study was made of clotting indices in dogs and their intercorrelation and relationship to human data. The most useful criterion for monitoring coagulation in experimental extracorporeal systems was sought. Linear regression and correlation analysis indicated that activated partial thromboplastin time (APTT) predicted whole blood clotting time with a correlation of 0.77 (p less than 0.01). Changes in the APTT with time after heparinization were similar to those previously reported in man, making the animal model an acceptable one for use in developing extracorporeal systems such as the membrane oxygenator. When blood activated recalcification time (BART), APTT, and whole blood clotting time (WBCT) assays were compared on the basis of applicability to studies of extracorporeal support, the APTT and the BART assays proved superior to the WBCT assay due to their reduced variability and increased speed of determination. The variability of the BART assay was the lowest, and its sensitivity was the same as the APTT assay. The principal drawback to the BART assay was not experienced in this study; that is, its dependence on adequate platelet levels which are unpredictable in extracorporeal systems.

Animals↗
PubMed1975

Oestrogen receptors in chick oviduct. Characterization and subcellular distribution.

Macromolecular components with properties of oestrogen receptors have been identified in the 0.5 M KCl nuclear soluble, the nuclear insoluble and the cytosol fractions of laying hen and immature (2--4 weeks, untreated by hormone) chicken oviduct. 7n the 0.5 M KCl extract of laying hen oviduct nuclei, a receptor, of protein nature according to the effects of enzymic treatments, has been identified. It exhibits high affinity for oestradiol with an apparent equilibrium association constant KA = 4 - 109 M-1 at 4 degrees C. The binding of [3H] oestradiol is abolished by 1 muM oestriol, oestrone and diethylstilboestrol, but not by the same concentration of progesterone, testosterone, and cortisol. Sucrose gradient ultracentrifugation studies in the presence of 0.5 M KCl indicate a sedimentation coefficient of 4.3 S, and there is partial aggregation in low-ionic-strength medium. The estimated number of binding sites per nucleus is about 5000, as calculated from DNA content of chick diploid genome. Most of the binding sites were found to be occupied by endogenous oestrogen(s). Oestradiol dissociates from the receptor according to an apparent two-step mechanism. The half-life time for the faster dissociation step is 18 h at 0 degrees C, 25 min at 20 degrees C and 10 min at 30 degrees C, and for the slower one is 180 h, 115 min and 60 min, respectively. In the 0.5 M KCl extract of immature chicken oviduct nuclei, there are approximately 500 receptor sites per nucleus; their affinity for oestradiol is the same as in the case of laying hen soluble nuclear receptor. After repeated extractions of nuclei with 0.5 M KCl medium, a substantial quantity of oestrogen binding sites remains in the residual fraction. Binding characteristics of this insoluble nuclear receptor resemble those of the soluble nuclear receptor: high affinity for oestradiol (KA = 7 - 10(8) M-1 at 37 degrees C) and specificity for oestrogens. The estimated number of binding sites are approximately 2000/cell for laying hen, and approximately 1000/cell for immature chicken. In the high-speed supernatant fraction of laying hen oviduct homogenates, an oestrogen receptor is also present, but its concentration is low (less than or equal to 100 sites/cell) and at the limits of sensitivity of the methods used. In the cytosol of immature chicken oviduct, there are approximately 2500 oestradiol receptor sites per cell.

Animals↗
PubMed1975

Histones H2a, H2b, H3, and H4 form a tetrameric complex in solutions of high salt.

In 2 M NaCl, histones H2b, H2a, H3, and H4 form a heterotypic tetrameric complex made up of one chain of each histone. This complex has been analyzed by hydrodynamic techniques. It is indistinguishable from histones in chromatin by its resistance to trypsin, pattern of reactivity with 125I. and ability to form specific crosslinked products after treatment with formaldehyde. It is proposed that this complex is responsible for protecting the small DNA fragments produced by exhausting nuclease digestion of nuclei and that on the average two of these complexes protect the larger 180-200 base pair unit produced by partial treatment of nuclei with nuclease.

Animals↗
PubMed1975

Identification of specific crosslinked histones after treatment of chromatin with formaldehyde.

Treatment of chromatin or nuclei with formaldehyde or glutaraldehyde results in the appearance of crosslinked histones as analyzed on SDS gels. The identity of two major crosslinked products was determined by iodinating the product and analzying the tryptic peptides. The results show that one product is a dimer of histones IIb2 and IIb1 and another product is a dimer of histones IIb2 and IV. These species represent no more than 15% of the total cellular histone.

Animals↗
PubMed1975

Pulmonary artery pressure and lung water during extracorporeal circulation in experimental pulmonary insufficiency.

Use of the membrane oxggenator has been advocated in the management of severe respiratory insufficiency. We have compared this method to conventional therapy in an experimental model in which 23 dogs were subjected to aspiration with 0.1 N HC1 and 18 were supported with a volume respirator and positive end-expiratory pressure or placed on partial bypass using a membrane oxygenator for 12 to 24 hours. Adequate oxygenation (POX greater than 100 mm Hg) was achieved with the membrane oxygenator. The increase in lung weight during conventional therapy was significantly greater than during membrane oxygenator support. Extracorporeal support during recovery from severe pulmonary injury allows pulmonary artery pressure to be controlled and reduces the expected increase in lung water.

Animals↗
PubMed1975

Rous sarcoma virus activates embryonic globin genes in chicken fibroblasts.

Complementary DNA (cDNA) specific for chick globin mRNA sequences fails to hybridize to total RNA extracted from chicken fibroblasts. After infection by Rous sarcoma virus, RNA complementary to globin cDNA is detectable in 100-500 copies per cell. Infection of fibroblasts with the transformation defective (td) deletion mutant of Rous sarcoma virus leads to normal virus production, but not to host cell transformation or accumulation of RNA sequences complementary to globin cDNA. Our evidence shows that the globin genes activated by Rous sarcoma virus are those specified by embryonic chick red cells; adult-specific globin sequences were not detected.

Age Factors↗
PubMed1975

Release of discrete subunits after nuclease and trypsin digestion of chromatin.

Digestion of chromatin with DNase (nucleate 3'-oligonucleotidohydrolase, EC 3.1.4.7) releases 11-12S nucleoprotein particles. After extensive nuclease digestion, the DNA in these particles consists of a collection of eight discrete DNA fragments. When these nuclease-particles are treated with trypsin (EC 3.4.21.4), only 20 to 30 amino-acid residues are cleaved from histone N-terminals, the histone C-terminal segments being resistant. The resulting 5S nucleoprotein particles have now been shown on acrylamide gels to consist of a series of eight discrete DNA-containing bands. Four of these bands contain C-terminal cleavage fragments from four histones (III, IV, IIb2, and IIb1) tightly bound to them; a fifth contains fragments from only histones III and IV. The remaining three bands contain only DNA. Since these protein-free DNA bands were resistant to nuclease prior to trypsin treatment, they were presumably associated with histone N-terminal segments in the native structure. Trypsin, therefore, appears to split nuclease-particles, releasing two subfractions of DNA--one associated with protein, the other not. The data is compatible with a model in which the majority of DNA in the eukaryotic nucleus is folded into hairpin loops of double-stranded helix, each created by the concerted cross-linking action of 6 to 10 histones which interact to form a trypsin-resistant complex composed, for the most part, of all four major histones. These loops may further fold upon themselves to form the "nu" bodies that have been visualized by electron microscopy.

Amino Acids↗
PubMed1974

Dissection of chromosome structure with trypsin and nucleases.

Exhaustive digestion of chromatin with trypsin leads to the cleavage of only 20-30 amino acids from each of histones III (f3), IV (f2a1), IIb2 (f2b), and IIb1 (f2a1), the remainder of these chains being resistant. This resistance is not altered by removing the histones from the DNA with 2 M NaCl, but is dramatically reduced in 6 M urea. Histones III, IV, IIb2, and possibly IIb1 are cleaved at their N-termini. Histones I and V and the nonhistone proteins are the first to be attacked by trypsin and have no detectable trypsin-resistant fragments. The arginine rich histones, III and IV, are then cleaved as a pair, followed by most of IIb2 and IIb1, also as a pair. This data is consistent with a model in which basic N-terminal "arms" extend from a trypsin-resistant histone complex. The structural arrangement of these arms relative to the trypsin-resistant histone complex may define the spatial coordinates of DNA binding sites and, consequently, the folding of the DNA fiber in the chromosome. Accompanying the tryptic digestion of the N-terminals of histones III, IV, IIb2, and possibly IIb1, is an increased sensitivity of chromatin to staphylococcal nuclease. As analyzed by electrophoresis, untrypsinized chromatin is digested into eight discrete limit-digest fragments by nuclease. Trypsinization results in the nuclease digestion of some, but not all, of these DNA bands. Together with the information on the way trypsin cleaves histones in chromatin, the analysis of the resistant DNA suggests that histone N-terminals are associated with some DNA bands and histone C-terminals with other DNA bands. We propose that histones fold the chromosome by crosslinking the DNA corresponding to these bands.

Animals↗