Determination of Oxygen Dosage Effects on Cytochrome Oxidase after Anoxia in Brain

Author(s):  
Fred Kriedt ◽  
Christopher Kriedt ◽  
Chase Patterson ◽  
Keith Van Meter
1985 ◽  
Vol 13 (4) ◽  
pp. 730-730 ◽  
Author(s):  
HEINZ REICHMANN ◽  
MARGARET A. JOHNSON ◽  
DOUGLASS M. TURNBULL ◽  
H. STANLEY A. SHERRATT

1986 ◽  
Vol 64 (2) ◽  
pp. 91-98 ◽  
Author(s):  
Michael A. Singer ◽  
Maria Dinda ◽  
Marlene Young ◽  
Leonard Finegold

Cytochrome oxidase was incorporated into liposomes, at various protein/lipid ratios, composed of either a phosphatidylcholine of varying chain length and symmetry or asolectin. Catalytic activity and respiratory control were assayed at two temperatures. All preparations showed higher activity at low protein/lipid ratios, but only asolectin showed respiratory control. A spectroscopic determination of the vectorial orientation of oxidase molecules showed that, for proteoliposomes with saturated lipids, 100% of oxidase molecules could be reduced by external substrate as compared with 75% for asolectin proteoliposomes. Freeze-fracture electron microscopy confirmed that oxidase was incorporated into these proteoliposomes and differential scanning calorimetry indicated that the protein induces significant disruption in the long range packing of the saturated phospholipids. We propose that the oxidase molecules in proteoliposomes formed from saturated phosphatidylcholines do not display respiratory control because they are unable to assume the transmembrane orientation necessary for full vectorial activity.


1978 ◽  
Vol 26 (3) ◽  
pp. 157-162 ◽  
Author(s):  
A C Frasch ◽  
M E Itoiz ◽  
R L Cabrini

Polyacrylamide models in which an extract of cattle heart mitochondria was incorporated, as well as cryostat sections of tongue muscle and epithelium, were used to set up the conditions under which the histochemical reaction for the demonstration of cytochrome oxidase can be quantitated. Using diaminobenzidine in a concentration of 5.5 mM, cytochrome C in a fixed concentration of 76 micron and keeping the incubation medium away from direct light action, enzyme activity can be evaluated by means of direct microphotometry on tissue sections. Each biologic model requires previous individual determination of the measurement limits. These limits can be readily established by using a small chamber for the incubation medium, which can be placed in the microphotometer, allowing the reaction rate to be following using a single section.


1949 ◽  
Vol 179 (2) ◽  
pp. 891-902 ◽  
Author(s):  
Frederick G. Smith ◽  
Elmer Stotz

Author(s):  
Tomas Najer ◽  
Ivo Papousek ◽  
Costica Adam ◽  
Alfred Trnka ◽  
Van Thi Quach ◽  
...  

One species of the louse genus Philopterus Nitzsch, 1818 is redescribed and illustrated: Philopterus acrocephalus Carriker, 1949 ex Acrocephalus luscinius (Quoy & Gaimard, 1830), A. melanopogon (Temminck, 1823), A. scirpaceus (Hermann, 1804), A. schoenobaenus (Linnaeus, 1758), Iduna aedon rufescens Stegmann, 1929, I. rama (Sykes, 1832), Locustella sp. and L. ochotensis (von Middendorff, 1853). Philopterus acrocephalus represents the first species of the Philopterus-complex recorded in the family Locustellidae Bonaparte, 1854. Philopterus gustafssoni sp. nov. is described ex Regulus regulus (Linnaeus, 1758), R. regulus regulus (Linnaeus, 1758), R. regulus azoricus Seebohm, 1883, R. regulus buturlini von Loudon, 1911, R. regulus sanctaemariae Vaurie, 1954, R. regulus tristis Pleske, 1892 and R. ignicapillus (Temminck, 1820). Descriptions of both species are amended with genetic data, DNA sequences of mitochondrial cytochrome oxidase I, nuclear hyp and TMEDE6; concatenated sequences are compared to the morphologically nearest species with genetic data available, Philopterus citrinellae (Schrank, 1776) and Philopterus fringillae (Scopoli, 1772). Holotype of Philopterus reguli (Denny, 1842) is pronounced to be a straggler, determination of other known material from Regulidae is changed for Philopterus gustafssoni sp. nov.


1978 ◽  
Vol 173 (3) ◽  
pp. 799-810 ◽  
Author(s):  
G M Clore ◽  
E M Chance

1. The results of non-linear optimization studies on the mechanism of reaction of fully reduced cytochrome oxidase with O2 at 176K are presented. The analysis is carried out on data obtained by means of dual-wavelength multi-channel spectroscopy at three wavelength pairs (604-630, 608-630 and 830-940 nm) and at three O2 concentrations (60, 200 and 1180 micron). The only model that satisfies the triple requirement of a standard deviation within the standard error of the experimental data, good determination of the optimized parameters and a random distribution of residuals is a three-species sequential mechanism. 2. On the basis of the optimized values of the relative absorption coefficients of the intermediates at each wavelength obtained from the present paper together with data from low-temperature trapping, e.p.r. and magnetic-susceptibility studies, the possible valence states of the metal centres in each of the intermediates are discussed.


Sign in / Sign up

Export Citation Format

Share Document