delta-Aminolevulinate dehydratase in human erythroleukemia cells: an immunologically distinct enzyme

Blood ◽  
1985 ◽  
Vol 65 (4) ◽  
pp. 939-944 ◽  
Author(s):  
CS Chang ◽  
S Sassa
Keyword(s):  
Butyric Acid ◽  
Deae Cellulose ◽  
K562 Cells ◽  
Normal Adult ◽  
Erythroleukemia Cells ◽  
Normal Enzyme ◽  
Normal Human ◽  
Dehydratase Activity ◽  
Ala Dehydratase ◽  
Selenium Oxide

Abstract Physicochemical and immunologic properties of delta-aminolevulinate (ALA) dehydratase in human K562 erythroleukemia cells were examined. ALA dehydratase activity was found to increase in K562 cells after treatment with butyric acid or selenium oxide. Enzyme activity in untreated K562 cells was comparable to that in normal adult erythrocytes but was increased three- to six-fold in K562 cells treated with 1.2 mmol/L butyric acid or 0.03 mmol/L selenium oxide. The Michaelis-Menten constant (Km), the inhibitor constant (Ki), and elution profile by diethylaminoethyl (DEAE) cellulose chromatography were similar for ALA dehydratase from K562 cells and normal human adult and human fetal erythrocytes. However, ALA dehydratase from K562 cells did not react with a monospecific rabbit antibody against ALA dehydratase purified from normal adult erythrocytes, although the antibody reacted with the enzyme from normal adult and fetal red cells. These findings indicate that ALA dehydratase in K562 cells is immunologically distinct from the normal enzyme.

scholarly journals delta-Aminolevulinate dehydratase in human erythroleukemia cells: an immunologically distinct enzyme

Blood ◽  
1985 ◽  
Vol 65 (4) ◽  
pp. 939-944
Author(s):  
CS Chang ◽  
S Sassa
Keyword(s):  
Butyric Acid ◽  
Deae Cellulose ◽  
K562 Cells ◽  
Normal Adult ◽  
Erythroleukemia Cells ◽  
Normal Enzyme ◽  
Normal Human ◽  
Dehydratase Activity ◽  
Ala Dehydratase ◽  
Selenium Oxide

Physicochemical and immunologic properties of delta-aminolevulinate (ALA) dehydratase in human K562 erythroleukemia cells were examined. ALA dehydratase activity was found to increase in K562 cells after treatment with butyric acid or selenium oxide. Enzyme activity in untreated K562 cells was comparable to that in normal adult erythrocytes but was increased three- to six-fold in K562 cells treated with 1.2 mmol/L butyric acid or 0.03 mmol/L selenium oxide. The Michaelis-Menten constant (Km), the inhibitor constant (Ki), and elution profile by diethylaminoethyl (DEAE) cellulose chromatography were similar for ALA dehydratase from K562 cells and normal human adult and human fetal erythrocytes. However, ALA dehydratase from K562 cells did not react with a monospecific rabbit antibody against ALA dehydratase purified from normal adult erythrocytes, although the antibody reacted with the enzyme from normal adult and fetal red cells. These findings indicate that ALA dehydratase in K562 cells is immunologically distinct from the normal enzyme.

INHIBITION BY HUMAN SERUM OF THE ADIPOKINETIC EFFECT OF A HUMAN PITUITARY LIPID-MOBILIZING FACTOR

1972 ◽  
Vol 71 (3) ◽  
pp. 443-453 ◽  
Author(s):  
Olav Trygstad ◽  
Irene Foss
Keyword(s):  
Human Serum ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Inhibitory Effect ◽  
Disc Electrophoresis ◽  
Inhibitory Protein ◽  
Human Pituitary ◽  
Albumin Fraction ◽  
Pituitary Glands ◽  
Normal Human

ABSTRACT A lipid-mobilizing factor (LMF) with an adipotrophic effect in human and animal fat tissue has been prepared from human pituitary glands. The addition of normal human serum to LMF reduced its lipolytic effect, and it was completely abolished by serum from a group of obese patients, whereas the lipolysis was not influenced by serum from patients with generalized lipodystrophy. By DEAE-cellulose chromatography of human serum the inhibitory effect on LMF was found to be present in a protein fraction less acidic than the main serum albumin fraction. The inhibitory fraction was deprived of some contaminants by Sephadex gel filtration. Disc electrophoresis demonstrated the presence of three components in the inhibitory protein (IP), and they were identified as albumin, transferin, and haemopexin by immuno-electrophoresis. Precipitation of these proteins by their rabbit antisera demonstrated that the inhibitory effect was present in the albumin fraction. Insulin like activity was not observed in IP. A protein binding of LMF by IP could not be demonstrated. Incubation at 37°C for one hour of a mixture of LMF and IP eliminated the electrophoretic picture of LMF. It is concluded that the inhibitory effect of human serum may be due to proteolysis of LMF.

ALA-dehydratase activity inZea mays L.

1985 ◽  
Vol 85 (3) ◽  
pp. 337-343 ◽  
Author(s):  
Luciano Scarponi ◽  
Piero Perucci ◽  
Mario Monotti
Keyword(s):  
Dehydratase Activity ◽  
Ala Dehydratase

scholarly journals Globin synthesis in mouse erythroleukemia cells in vitro: a switch in beta chains due to inducing agent

Blood ◽  
1977 ◽  
Vol 50 (5) ◽  
pp. 867-876 ◽  
Author(s):  
BP Alter ◽  
SC Goff
Keyword(s):  
Protein Synthesis ◽  
Butyric Acid ◽  
Cell System ◽  
Globin Chain ◽  
Erythroleukemia Cells ◽  
Friend Cells ◽  
Erythroleukemia Cell ◽  
Globin Synthesis ◽  
Mouse Erythroleukemia

Abstract Friend erythroleukemia cells, originally derived from DBA/2 mice, differentiate when cultured with inducing agents. Studies of the different effects of inducing agents on clone 745 have revealed that both dimethyl sulfoxide (DMSO) and hemin produce benzidine-positive cells. Butyric acid produced mature but benzidine-negative cells in this clone. All agents induced globin synthesis above the 0.1% of protein synthesis found in uninduced cells. DMSO induction stimulated globin synthesis 9%, hemin 2%, and butyric acid 3%. Total beta/alpha ratios were approximately unity with all agents. Although the inducing agents all stimulated total globin synthesis in Friend cells, the relative rates of synthesis of the two mouse beta chains were affected differently by the various agents. Hemin markedly increased the proportion of beta minor. For example, DBA/2 mouse reticulocytes synthesized 20% beta minor and 80% beta major. DMSO induction of clone 745 caused 20%-33% synthesis of beta minor. In contrast, hemin increased the proportion of beta minor to 64%-69%. Thus the Friend erythroleukemia cell system provides an in vitro approach to the study of the regulation of globin-chain switching.

Induction of Globin Gene Expression in Cultured Erythroleukemia Cells by Butyric Acid

1977 ◽  
Vol 81 (6) ◽  
pp. 1901-1910 ◽  
Author(s):  
Reiko KAMEJI ◽  
Masuo OBINATA ◽  
Yasuo NATORI ◽  
Yoji IKAWA
Keyword(s):  
Gene Expression ◽  
Butyric Acid ◽  
Globin Gene ◽  
Erythroleukemia Cells ◽  
Globin Gene Expression

scholarly journals Effects of variant gamma chains and sialic acid content of fibrinogen upon its interactions with ADP-stimulated human and rabbit platelets

Blood ◽  
1984 ◽  
Vol 64 (6) ◽  
pp. 1163-1168 ◽  
Author(s):  
EJ Harfenist ◽  
MA Packham ◽  
JF Mustard
Keyword(s):  
Sialic Acid ◽  
Acid Content ◽  
Deae Cellulose ◽  
Adenosine Diphosphate ◽  
Gamma Chain ◽  
Sialic Acid Content ◽  
Human Fibrinogen ◽  
Rabbit Platelets ◽  
Chain Composition ◽  
Normal Human

Abstract When platelets are stimulated with adenosine diphosphate (ADP), fibrinogen binds to receptors on the platelet membrane, and the platelets aggregate. The primary platelet recognition sites of human fibrinogen are reported to be at the COOH-terminal ends of the gamma chains, with secondary sites in the A alpha chains. Normal human fibrinogen, which consists of three pairs of disulfide-bonded peptide chains, (A alpha, B beta, gamma)2, is heterogeneous with respect to sialic acid content and also contains a small proportion of molecules with a variant gamma chain (designated gamma'), elongated by a peptide extension at the COOH-terminus of the normal gamma chain. We separated fibrinogen into three fractions by chromatography on DEAE cellulose and tested the interactions of these fractions with ADP-stimulated human and rabbit platelets. Two fractions had the normal chain composition, (A alpha B beta, gamma)2, but different sialic acid contents (6.6 and 7.2 mol/mol), and the third fraction had the chain composition (A alpha, B beta)2 gamma gamma' and a sialic acid content of 7.2 mol/mol, which is similar to that of one of the normal fractions. In binding and aggregation experiments, we detected no significant differences between the reactions of the first two fractions, but ADP-stimulated platelets bound only 50% as much of 125I-fibrinogen from the fraction with the gamma' chains and also aggregated less extensively in the presence of this fraction. We conclude that the sialic acid content of fibrinogen does not significantly affect its interactions with platelets, but the elongated gamma' chains bind less effectively to ADP-stimulated platelets, and thus reduce the ability of fibrinogen to support aggregation. This may result from a conformational change caused by the gamma' extension or from the deletion of a portion of the normal gamma chain recognition site.

Effect of Ethanol and Zinc on ALA-Dehydratase Activity in Red Blood Cells

Enzyme ◽  
1976 ◽  
Vol 21 (3) ◽  
pp. 248-252 ◽  
Author(s):  
M. Abdulla ◽  
Brigitta Haeger-Aronsen ◽  
S. Svensson
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Dehydratase Activity ◽  
Ala Dehydratase

scholarly journals The chemical constitution of the proteoglycan of human intervertebral disc

1976 ◽  
Vol 157 (3) ◽  
pp. 753-763 ◽  
Author(s):  
R H Pearce ◽  
B J Grimmer
Keyword(s):  
Chondroitin Sulphate ◽  
Deae Cellulose ◽  
Intervertebral Discs ◽  
Guanidinium Chloride ◽  
Keratan Sulphate ◽  
Qualitative And Quantitative ◽  
Cscl Density Gradient ◽  
Chemical Constitution ◽  
Normal Human ◽  
Quantitative Analyses

Proteoglycan was prepared from three pools of normal human intervertebral discs by extraction with buffered 4M-guanidinium chloride followed by CsCl-density-gradient ultracentrifugation. Chromatography on agarose (Bio-Gel A-150m) and on DEAE-cellulose suggested a single polydisperse proteoglycan species. The intrinsic viscosities of three preparations were 166, 122 and 168 ml/g. After degradation with 0.5M-KOH containing 0.02M-NaBH4, the glycosaminoglycans were recovered quantitatively and their Ca2+ salts separated into a hexuronate-rich fraction (fraction 1), which was precipitated in 0-45% (v/v) ethanol, and a hexose-rich fraction (fraction2), which was precipitated in 45-70% (v/v) ethanol. Qualitative and quantitative analyses of the glycosaminoglycans revealed fraction 1 to be chondroitin sulphate, and fraction 2 to be keratan sulphate; the latter was contaminated with protein and possibly a small amount of another glycosaminoglycan. For both glycosaminoglycans, plots of log(mol.wt.) against weight fell close to a normal distribution. The mode for chondroitin sulphate was close to 20000; that for keratan sulphate, 10000. A threefold range of molecular weight included the central 16-84% [+/- 1 S.D. of log(mol.wt.)] of the weight of both fractions.

Normal human gingival fibroblasts undergo cytostasis and apoptosis after long-term exposure to butyric acid

2017 ◽  
Vol 482 (4) ◽  
pp. 1122-1128 ◽  
Author(s):  
Michihiro Shirasugi ◽  
Keisuke Nishioka ◽  
Toshiro Yamamoto ◽  
Takaaki Nakaya ◽  
Narisato Kanamura
Keyword(s):  
Butyric Acid ◽  
Human Gingival Fibroblasts ◽  
Gingival Fibroblasts ◽  
Normal Human
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