Investigation of the Flammability Properties of Hydraulic Fluids

Wright, B.R.; Weatherford, W. D.; Pera, Maurice E. Le

doi:10.21236/ada019775

Cited by 21 publications

(32 citation statements)

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“…The monomeric state of H 1 has led to proposals that its function is quite separate from that of the other histones and this may also be true for H5. In chicken erythrocytes the stoichiometry of histones H 5 and H 1 together, with respect to the other four histones, appears to be similar to that of H 1 alone in calf thymus [7,29].A number of spectroscopic techniques are applied here to establish the presence and nature of secondary and tertiary structure in H 5 and preliminary attempts to determine the position of the structured region have …”

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Structural Studies of Chicken Erythrocyte Histone H5

Crane‐Robinson

Danby

Bradbury

et al. 1976

European Journal of Biochemistry

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Spectroscopic studies (nuclear magnetic resonance, circular dichroism and infrared) have been carried out on chicken erythrocyte histone H 5 and on three peptides cleaved therefrom: 1-31, 32-197 and 58-197. It is shown that at ionic strengths above 0.1M part of the H 5 molecule takes up a globular conformation containing 14% a helix but no p sheet structure. Several details of the circular dichroism and nuclear magnetic resonance spectra indicate that the globular region is located in the N-terminal half of the molecule and this proposal is supported by the observation that the peptide 32-197 is largely incapable of folding and the peptide 59-197 is completely incapable of folding. Structural similarities and differences between histone H 5 and histone H 1 are discussed.The nucleated erythrocytes of birds, reptiles, amphibians and fish contain a very basic histone, H5, that has not been found in other tissues [l -51. H 5 largely, but not completely, replaces H 1 and the two histones are not dissimilar in amino acid composition and molecular weight [4,6 -81. A significant difference between the two histones is that H 5 contains 11 % arginine whilst H 1 contains only 2%. In this respect H 5 resembles the 4 1 histones of marine invertebrate sperm (in particular sea urchins) which totally replace the H I and also contain about 11% arginine in addition to roughly 25% lysine 191. Early observations of the occurrence and composition of H 5 resulted in the suggestion that its function is the total suppression of the genome in the fully mature erythrocyte [lo]. Detailed studies on anemic chickens have subsequently shown, however, that H 5 can be detected even in erythroblasts (when a wide range of protein synthesis is taking place), and does not appear suddenly at the mature erythrocyte stage when protein synthesis is finally terminated [I 1 -151. The function of H 5 in relation to genome suppression is, therefore, not as simple as originally thought. H 5 nevertheless is closely related to H I [I61 and a number of experiments have implicated H 1 in the condensation of diffuse chromatin [17 -191. In particular the state of chromatin is thought to depend on the degree of phosphorylation of H 1 [20,21] and recently it has been shown that H 5 is phosphorylated and dephosphorylated in viuo [22]. There is at present no evidence to Abbreviations. NMR, nuclear magnetic resonance; CD, circular dichroism.suggest why H 1 should be replaced in large part by H 5 and the present structural investigation of H 5 was carried out to point out the similarities and differences between H 5 and H 3 . Related studies on H 1 have already been published [23,24]. Hydrodynamic studies have shown that H 5 does not aggregate at high ionic strength [8,28] and thereby resembles H 1 and not the remaining four histone fractions. The monomeric state of H 1 has led to proposals that its function is quite separate from that of the other histones and this may also be true for H5. In chicken erythrocytes the stoichiometry of histones H 5 and H 1 together, wi...

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confidence: 99%

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confidence: 99%

Structural Studies of Chicken Erythrocyte Histone H5

Crane‐Robinson

Danby

Bradbury

et al. 1976

European Journal of Biochemistry

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“…This period is also confirmed by published postdiscovery photometry. Detailed analysis by Wright et al (1975) of 1068 photographic observations of Sco X-1 from Harvard plate collections, as well as 698 postdiscovery magnitudes confirm the period. Moreover it shows that its B magnitude ranges between 11.8 and 13.7 mag.…”

Section: Photometric Propertiesmentioning

confidence: 77%

Sco X-1

Miyamoto

Matsuoka

1977

Space Sci Rev

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Abstract. The physical properties of X-ray, optical and radio emissions from Sco X-1 are reviewed. Sco X-I is a typical X-ray source which has an optically thick hot plasma. The observational spectra of X-ray and optical emissions are consistent with theoretical ones from the hot plasma, but the radio emission shows a non-thermal feature. The restrictive conditions for the model of Sco X-1 are discussed from the observational facts. In spite ot numerous observational facts on Sco X-1 further detailed and elaborate studies are necessary to understand this object and general compact X-ray sources comprehensively.Contents:

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“…However, the Cannizzaro reaction is well recognized to proceed for aldehydes with no α-hydrogen [8]. Furthermore, the Swern oxidations of vicinal diols 18 [9], 19 [10] and 20 [11] have all been reported to give the corresponding α-diketones, as did the oxidation reaction of 6. Thus, from our results we did not obtain evidence to discriminate between those reaction pathways and other potential mechanisms for the present reaction might be considered.…”

Section: Methodsmentioning

confidence: 99%