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106. THE EFFECT OF LARGE DOSES OF THIOUREA ON THE COMPOSITION OF THE LIVER AND URINE OF RATS

Author

DOLJANSKI, F., ESHKOL, Z., GIVOL, D., KAUFMANN, E., and MARGOLIASH, E.

Abstract

Following the observation that large daily doses of thiourea induced numerous mitoses in the liver of rats [Rachmilewitz, Rosin & Doljanski, 1950], the concomitant chemical changes in the liver and urine of thiourea-treated rats were investigated. It was found that:(1) The mitogenetic reaction, which occurred on the 3rd day of treatment with the drug, was preceded by (a) a decrease in liver catalase activity to 30–50% of the normal within 12 hr; (b) an increase in total liver weight and concentration of liver ribonucleic acid within 2 days. The enlarged liver was normal with respect to protein, lipid, water and deoxyribonucleic acid content.(2) The concentration of liver glycogen decreased markedly on the 1st day of thiourea treatment but returned to normal by the 2nd or 3rd day.(3) During the period of treatment with thiourea there was an increase in the urinary excretion of uric acid, allantoin, and phosphate, as well as glucosuria and polyuria. There was no change in the excretion of urea and total sulphate.(4) All these changes, both in the liver and the urine, were fully reversible on withdrawing the drug.

Published
1956
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107. The primary structure of cytochrome c from the rust fungus Ustilago sphaerogena

Author

Bitar, K. G., Vinogradov, S. N., Nolan, C., Weiss, L. J., and Margoliash, E.

Abstract

1. The complete amino acid sequence of cytochrome c from the basidiomycete Ustilago sphaerogena was determined from the amino acid compositions and sequences of either tryptic or chymotryptic peptides, and in homology with at least thirty other established sequences of cytochrome c. 2. The primary structure of the molecule bears all of the characteristics of a mammalian-type cytochrome c, showing the typical clustered distribution of hydrophobic and basic residues with a single polypeptide chain of 107 residues. 3. Like all other fungal cytochromes c, it possesses a free N-terminus, and one less residue at the C-terminus than vertebrate cytochromes c. The region of residues 70–80 is strictly conserved, as is histidine at position 18. Position 26 is occupied by an asparagine residue, in contrast to histidine which occurs at this location in most of the known sequences of mammalian-type cytochromes c. 4. In contrast to some other fungal and plant cytochromes c of known primary structures, the Ustilago cytochrome c molecule does not contain trimethyl-lysine. 5. The sequence of Ustilago cytochrome c differs from the sequences of human, horse, chicken, tuna, wheat, and baker's yeast proteins at loci 47, 43, 44, 44 and 38 respectively.

Published
1972
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110. Separate Intramolecular Pathways for Reduction and Oxidation of Cytochrome cin Electron Transport Chain Reactions

Author

Margoliash, E., Ferguson-Miller, Shelagh, Tulloss, J., Kang, Chae Hee, Feinberg, B. A., Brautigan, D. L., and Morrison, M.

Abstract

The monoiodotyrosine 74, formyltryptophan 59, mononitrotyrosine 67, and carboxymethylmethionine 80 derivatives of horse cytochrome care defective in their ability to accept electrons from the succinate-cytochrome creductase system, while their reactions with purified cytochrome coxidase are essentially those of the native protein. The 4-nitrobenzo-2-oxa-1,3-diazole derivative of lysine 13 of horse cytochrome cand the bis-phenylglyoxal derivative of arginine 13 of Candida kruseicytochrome chave the opposite properties, in that they are readily reduced by the succinate-cytochrome creductase (EC 1.3.99.1) system but are defective in their capability of transferring electrons to cytochrome coxidase (EC 1.9.3.1). We conclude that electrons from mitochondrial cytochrome creductase are transmitted to ferricytochrome cby a different pathway than electrons from ferrocytochrome cto cytochrome coxidase. The present results are compatible with the concept that the mechanism of reduction involves an aromatic ring channel comprising residues 74, 59, 67, and 80, leading from the “left back” part of the protein to the heme iron. On the other hand, since residue 13 is immediately above the edge of the heme that is at the “front surface” of the molecule, we suggest that the electron leaves ferrocytochrome cto cytochrome coxidase by way of the edge of pyrrole ring II or the adjacent surface-located sulfur of cysteinyl residue 17, which is thioether bonded to the heme. On this basis, the sites of electron entry and exit in cytochrome cwould appear to be some 110° of arc away from each other along the surface of the protein, explaining several previously observed phenomena.

Published
1973
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113. Time dependence of B cell processing and presentation of peptide and native protein antigens

Author

Ek, Lakey, La, Casten, Wl, Niebling, Margoliash E, and Sk, Pierce

Subjects
B-Lymphocytes, T-Lymphocytes, Lymphocyte Cooperation, Antigen-Presenting Cells, Proteins, Cytochrome c Group, Lymphocyte Activation, Antibodies, Anti-Idiotypic, Kinetics, Mice, Mice, Inbred CBA, Animals, Female, Antigens, Columbidae, Peptides
Abstract

Th cell recognition of globular proteins requires the uptake and intracellular processing of the native Ag by an APC to produce a peptide fragment containing the T cell antigenic determinant, which is recognized in conjunction with Ia. This report describes the time course of the processing and presentation of a soluble globular protein Ag, pigeon cytochrome c (Pc), and of the presentation of a C-terminal peptide fragment of Pc, residues 81 to 104 (Pc 81-104), which does not require processing. Splenic B cells, acting as APC, require 6 to 8 h incubation with native Pc to process and present it to an I-Ek-restricted Pc-specific T cell hybrid, resulting in the secretion of IL-2. Moreover, the time required for B cells to process Pc is the same whether the Ag is taken up by nonspecific fluid phase pinocytosis or by binding to surface Ig. Once processed, Ag is lost from the B cell surface by 8 to 12 h, although when provided with fresh Pc, the same B cells are still capable of processing and presenting. In contrast to native Pc, only 1 to 2 h are required for the peptide fragment Pc 81-104 to become associated with B cells in a stimulatory fashion, and this time is similar for live and paraformaldehyde-fixed B cells, which cannot internalize or process the peptide. Washed free of excess peptide after 2 h, B cells lose their ability to stimulate T cells by 8 to 12 h, with a time course indistinguishable from that for the loss of processed native Pc. Prolonged incubation of B cells with the peptide for 18 to 24 h results in a dramatic loss of the ability to present Pc 81-104. Even when provided with fresh Pc or Pc 81-104, these cells have diminished ability to present these Ag. This loss is selective, inasmuch as these B cells remain equivalent to untreated B cells in the presentation of an unrelated Ag, OVA, to an I-Ak-restricted specific T cell. However, the ability to present another I-Ek-restricted antigenic peptide of the D glycoprotein of HSV to its specific T cell is also diminished. Loss of activity is observed after incubation only with the peptide and not with the native protein and is not due to a depletion of the antigenic peptide from the incubation medium.(ABSTRACT TRUNCATED AT 400 WORDS)

Published
1988

114. Six related protein products from a single patient with multiple myeloma

Author

Margoliash E, Byron E. Anderson, Anderas P, Kaplan B, Jemmerson R, and Denton

Subjects
Oncology, Male, medicine.medical_specialty, Myeloma protein, Carbohydrates, Immunoglobulin Variable Region, Biochemistry, Immunoglobulin Fab Fragments, Immunoglobulin kappa-Chains, Text mining, Internal medicine, medicine, Humans, Amino Acid Sequence, Amino Acids, Multiple myeloma, Chemistry, business.industry, Middle Aged, medicine.disease, Peptide Fragments, Single patient, Molecular Weight, Myeloma Proteins, Immunoglobulin G, Immunoglobulin Light Chains, Binding Sites, Antibody, business, Multiple Myeloma
Published
1979

116. Proinsulin and the Biosynthesis of Insulin

Author

Nolan C, Arthur H. Rubenstein, J.L. Clark, Donald F. Steiner, Margoliash E, Aten B, and Philip E. Oyer

Subjects
chemistry.chemical_compound, Biosynthesis, chemistry, Biochemistry, Insulin, medicine.medical_treatment, medicine, Proinsulin
Published
1969
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120. Primary structure of mouse, rat, and guinea pig cytochrome c

Author

Carlson, Steven S., primary, Mross, George A., additional, Wilson, Allan C., additional, Mead, Robert T., additional, Wolin, Lawrence D., additional, Bowers, Steven F., additional, Foley, Neal T., additional, Muijsers, A. O., additional, and Margoliash, E., additional

Published
1977
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