Search PubMed⌕ Search

Biomedical subjects

E Eigenbrodt

Publications and source records attributed to E Eigenbrodt.

At least 73 records · Page 4Linked to original sources
PubMed1980

Localization of anti-mitochondrial antibody in experimental canine myocardial infarcts.

Alterations in cell and subcellular membrane integrity occur during evolving ischemic myocardial injury. We tested the hypothesis that an antibody against human liver mitochondria [anti-mitochondrial antibody developing in a patient with primary biliary cirrhosis] could identify altered cell membrane integrity in experimental canine myocardial infarcts. The proximal left anterior descending coronary arteries of 12 dogs were ligated and 1 hr later 131I-labeled F(ab')2 fragments from either a control human IgG (6 dogs) or anti-mitochondrial IgG (6 dogs) were injected. The 131I-labeled F(ab')2 anti-mitochondrial fragments concentrated maximally in the central infarct subendocardium [infarct-to-normal ratio of 9.2 +/- 3.5 (mean +/- SD) vs. 4.6 +/- 3.3 for control F(ab')2 IgG, P < 0.05]. There was also 1 1/2- to 2-fold greater anti-mitochondrial antibody F(ab')2 accumulation in the central infarct epicardium and the peripheral infarct subendocardium and subepicardium. Thus, an anti-mitochondrial antibody obtained from a patient with primary biliary cirrhosis concentrates in irreversibly damaged myocardium after experimental canine myocardial infarction. Presumably this occurs because of altered cell membrane integrity, which allows exposure of mitochondria to the anti-mitochondrial antibody. The F(ab')2 fragments of anti-mitochondrial antibodies labeled with suitable radionuclides should allow noninvasive scintigraphic detection of experimental acute myocardial infarcts.

Animals↗
PubMed1979

Immunohistochemical localization of pyruvate kinase isoenzymes in chicken tissues.

A method for the localization of pyruvate kinase isoenzymes type L, M2 and M1 in tissue sections is described. Mono-specific antibodies directed against isoenzymes of pyruvate kinase from chicken and the peroxidase antiperoxidase method were used. The following preferential localizations of the isoenzymes in chicken tissues were observed: Pyruvate kinase M1 was found in skeletal muscle. The white muscle fibers were more intensely stained than the red. Some dark muscles (e.g., anterior latissimus dorsi) and the heart muscle showed no reaction with antiserum against pyruvate kinase M1. Pyruvate kinase type L was found in the hepatocytes and in kidney cortex. Pyruvate kinase type M2 was seen in the distal tubules of kidney, in hepatocytes and sinusoidal cells in liver, in lung, adipose tissue, and in the spleen mainly in the bursa dependent areas. Pyruvate kinase type M2 was detected in high concentrations in the granulation tissue of regenerating liver after partial hepatectomy. Liver sections of a hen bearing a pancreatic tumor showed an unusually high content of pyruvate kinase type M2 in some hepatocytes, which were each clustered to spots in the liver parenchyma. Thus, contrary to previous reports, the tissue distribution of isoenzymes in chicken is similar to that of other vertebrates.

Animals↗
PubMed1979

Modification of pyruvate kinase activity by proteins from chicken liver.

The partial purification of a protein fraction inhibiting pyruvate kinase isoenzymes is described. The fraction was isolated from the (NH4)2SO4 step of the purification procedure for pyruvate kinase isoenzymes from chicken liver (Eigenbrodt, E. & Schoner, W. (1977) Hoppe-Seyler's Z. Physiol. Chem. 358, 1033-1046) by extraction with 1N NaOH, acidification to pH 3, ethanol precipitation and chromatography of the supernatant on DEAE-cellulose. The inhibitor fraction was further purified by disc gel electrophoresis using a gel gradient from 10 to 25%; this procedure separated activating proteins from the inhibitor fraction. The inhibitor fraction inhibited the pyruvate kinase isoenzymes from chicken in the sequence of decreasing effect: M2 greater than L greater than M1. The inhibition was due to a decrease in the affinity for phosphoenolpyruvate. The inhibitor is stable against heating for 5 min in 1% sodium dodecyl sulfate at 100 degrees C; it is destroyed by pepsin digestion. The inhibitor fraction could be purified further only by dodecyl sulfate gel electrophoresis. This resulted in the separation of 2 inhibitors (Mr = 33,500 +/- 8500 and ca. 5000), an activator (Mr = 15,100 +/- 5200), and an unidentified protein (Mr = 27,000).

Animals↗
PubMed1978

Portal hypertension following renal transplantation.

Portal hypertension and variceal hemorrhage may be found in the renal transplant patient with chronic liver disease. The development of portal hypertension was found to occur after long-term graft survival without significant rejection. The development of positive cytomegalic virus and negative hepatitis-associated antigen appeared to be common. Splenomegaly and prominent venous collateral were the most frequent physical findings, while ascites and hepatomegaly were less frequent. Portasystemic decompression can be performed successfully, however, the mortality and morbidity appear to be higher for this group than for other cirrhotic patients with comparable hepatic reserve.

Adult↗
PubMed1977

Purification and properties of the pyruvate kinase isoenzymes type L and M2 from chicken liver.

A procedure for the simultaneous purification of both isoenzymes of pyruvate kinase (type M2 and L) from chicken liver has been worked out. Each isoenzyme produces a single band in dodecylsulfate gel electrophoresis. Each has a molecular weight of 190 000 and contains four apparently identical subunits of Mr = 50 000. The isoenzymes differ in their isoelectric points (type L: 6.3; type M2: 8.3) and their kinetic behaviour. Pyruvate kinase type L had an S-shaped phosphoenolpyruvate saturation curve (K 0.5=0.79 mM) which was transformed into an hyperbola in the presence of fructose 1,6-bisphosphate, while type M2 had a phosphoenolpyruvate saturation curve of the Michaelis-Menten type (K0.5=0.2mM). Antibodies against pyruvate kinase type L from chicken liver inactivated type L from rat and partially inactivated type M2 from chicken and rat; but the antibodies against type L did not react with type M1 from chicken breast muscle. It is therefore concluded that, contrary to a previous report (Strandholm, J.J. et al. (1975) Biochemistry 14, 2242-2246), avian liver contains pyruvate kinases type M2 and L as the mammalian liver does.

Adenosine Diphosphate↗
PubMed1977

Inactivation of pyruvate kinase type M2 from chicken liver by phosphorylation, catalyzed by a cAMP-independent protein kinase.

A cAMP-independent protein kinase from chicken liver phosphorylated and inactivated pyruvate kinase type M2 from the same tissue. Complete inactivation was reached when 4 mol of phosphate were incorporated/mol of tetrameric pyruvate kinase. The protein kinase bound with high affinity to pyruvate kinase type M2 (Km value for pyruvate kinase = 6 X 10(-10)M; it phosphorylated phosvitin and casein but not histones, ATP and GTP were substrates. The differences between the properties of this protein kinase in the interconversion of pyruvate kinase and that described previously are discussed.

Animals↗
PubMedDate not supplied

Renal infarction with absolute ethanol.

Selective renal artery catheterization was undertaken in a series of mongrel dogs. Absolute ethanol was injected on a dose/weight ratio. Venous blood ethanol levels were monitored. Pre- and postprocedure angiography was performed to evaluate the effectiveness of the injection. The dogs were subsequently sacrificed and pathologic examination performed. Renal infarction was produced in all animals. Systemic blood alcohol levels remained consistently below established criteria of toxic levels. No evidence of vascular damage in systemic arteries distal to the renal artery was found. Absolute ethanol is apparently a safe and effective method of producing permanent renal infarction.

Animals↗