egg-white and Leukemia--Myeloid

The association constants for the binding of various saccharides to hen egg-white lysozyme and human lysozyme have been measured by fluorescence titration. Among these are the oligosaccharides GlcNAc-beta(1 leads to 4)-MurNAc-beta(1 leads to 4)-GlcNAc-beta(1 leads to 4)-GlcNAc, GlcNAc-beta(1 leads to 4)-MurNAc-beta(1 leads to 4)-GlcNAc-beta(1 leads to 4)-N-acetyl-D-xylosamine, and GlcNAc-beta(1 leads to 4-GlcNAc-beta(1 leads to 4)-MurNAc, prepared here for the first time. The binding constants for saccharides which must have N-acetylmuramic acid, N-acetyl-D-glucosamine, or N-acetyl-D-xylosamine bound in subsite D indicate that there is no strain involved in the binding of N-acetyl-D-glycosamine in this site, and that the lactyl group of N-acetylmuramic acid (rather than the hydroxymethyl group) is responsible for the apparent strain previously reported for binding at this subsite. For hen egg-white lysozyme, the dependence of saccharide binding on pH or on a saturating concentration of Gd(III) suggests that the conformation of several of the complexes are different from one another and from that proposed for a productive complex. This is supported by fluorescence difference spectra of the various hen egg-white lysozyme-saccharide complexes. Human lysozyme binds most saccharides studied more weakly than the hen egg-white enzyme, but binds GlcNAc-beta(1 leads to 4)-MurNAc-beta(1leads to 4)-GlcNAc-beta(1 leads to 4)-MurNAc more strongly. It is suggested that subsite C of the human enzyme is "looser" than the equivalent site in the hen egg enzyme, so that the rearrangement of a saccharide in this subsite in response to introduction of an N-acetylmuramic acid residue into subsite D destabilizes the saccharide complexes of human lysozyme less than it does the corresponding hen egg-white lysozyme complexes. This difference and the differences in the fluorescence difference spectra of hen egg-white lysozyme and human lysozyme are ascribed mainly to the replacement of Trp-62 in hen egg-white lysozyme by Tyr-63 in the human enzyme. The implications of our findings for the assumption of superposition and additivity of energies of binding in individual subsites, and for the estimation of the role of strain in lysozyme catalysis, are discussed.

Topics: Acetylglucosamine; Animals; Chickens; Egg White; Female; Humans; Hydrogen-Ion Concentration; Kinetics; Leukemia, Myeloid; Ligands; Muramidase; Oligosaccharides; Protein Binding; Species Specificity; Spectrometry, Fluorescence

Topics: Amino Acid Sequence; Amino Acids; Animals; Chickens; Circular Dichroism; Egg White; Fluorescence; Humans; Hydrogen-Ion Concentration; Leukemia, Myeloid; Muramidase; Neoplasms, Experimental; Rats; Species Specificity; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine

Topics: Acetates; Acute Disease; Amino Acids; Animals; Binding Sites; Chemical Phenomena; Chemistry; Chickens; Circular Dichroism; Egg White; Glucosamine; Humans; Hydrogen-Ion Concentration; Leukemia, Myeloid; Mathematics; Mice; Muramidase; Protein Binding; Protein Conformation; Rats; Tryptophan; Tyrosine

Topics: Acetates; Binding Sites; Binding, Competitive; Chromatography, Ion Exchange; Egg White; Humans; Hydrogen-Ion Concentration; Leukemia, Myeloid; Mathematics; Muramidase; Oligosaccharides; Protein Binding; Quantum Theory; Spectrometry, Fluorescence; Spectrophotometry; Spectrophotometry, Ultraviolet

Topics: Acid Phosphatase; Agar; Alkaline Phosphatase; Amylases; Animals; Cattle; Chickens; Chromatography, Gel; Deoxyribonucleases; Diffusion; Egg White; Gels; Intestines; Kinetics; Leukemia, Myeloid; Macaca; Male; Methods; Muramidase; Pancreas; Plants; Polysaccharides; Ribonucleases; Semen; Swine; Triticum

Topics: Amino Acid Sequence; Amino Acids; Animals; Biological Evolution; Birds; Cellulose; Chickens; Chromatography, Gel; Chromatography, Ion Exchange; Complement Fixation Tests; Cross Reactions; Ducks; Egg White; Electrophoresis; Epitopes; Humans; Hydrogen-Ion Concentration; Immune Sera; Immunization; Immunodiffusion; Immunoelectrophoresis; Ion Exchange Resins; Leukemia, Myeloid; Male; Mathematics; Muramidase; Protein Conformation; Rabbits; Species Specificity; Time Factors; Turkeys; Ultracentrifugation

Topics: Egg White; Humans; Leukemia; Leukemia, Lymphoid; Leukemia, Myeloid; Leukocytes; Mass Screening; Muramidase; Pyelonephritis; Sarcoidosis; Tears; Tuberculosis

A transplantable mouse tumor, GPC-11, produces large amounts of lysozyme. The tumor is a reticulum cell sarcoma, type A, and is a neoplasm of monocytes. The lysozyme was purified from mouse urine in quantities sufficient for structural analysis. Comparison of mouse lysozyme with lysozymes from; chicken egg white and patients with monocytic leukemia reveals similarities in size and electrophoretic mobility and, with human lysozyme, in functional properties; but considerable differences are found in antigenic characteristics and amino acid composition.

Topics: Animals; Chromatography, Ion Exchange; Egg White; Electrophoresis; Humans; Hydrogen-Ion Concentration; Leukemia, Myeloid; Lymphoma, Large B-Cell, Diffuse; Mice; Monocytes; Muramidase; Ultracentrifugation

Topics: Egg White; Humans; Leukemia, Myeloid; Muramidase; X-Ray Diffraction

Lysozyme, isolated from the urine of patients with monocytic leu kemia, has been crystallized as the chlo ride at pH 4.5 and at pH 10.5. The crystal forms of the human enzyme show certain similarities as well as dis tinct dissimilarities compared with the crystal forms of lysozyme chloride from hen's egg white.

Topics: Crystallization; Egg White; Humans; Hydrogen-Ion Concentration; Leukemia, Myeloid; Muramidase