scholarly journals HUMAN AMYLOID PROTEIN: CHEMICAL VARIABILITY AND HOMOGENEITY

1971 ◽  
Vol 19 (1) ◽  
pp. 1-15 ◽  
Author(s):  
M. HARADA ◽  
C. ISERSKY ◽  
P. CUATRECASAS ◽  
D. PAGE ◽  
H. A. BLADEN ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amyloid Fibril ◽  
Gel Filtration ◽  
Protein S ◽  
Amyloid Protein ◽  
X Ray Diffraction ◽  
Amyloid Proteins ◽  
X Ray ◽  
Chemical Variability ◽  
Sepharose 4B

The morphology of the fibril of amyloid derived from different individuals is similar, but occasionally significant differences are noted. All human amyloid filaments have a "β-pleated sheet" conformation as revealed by x-ray diffraction, and those examined after orientation show a "cross-β" pattern. All amyloid fibril concentrates studied so far can be fractionated to obtain the major amyloid protein component(s) by sequential gel filtration with 5 M guanidine-HCl in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns with the removal of over 28% of proteins representing minor constituents. The major amyloid protein(s) obtained from the spleen and/or liver of six patients is found to contain tryptophan, to be deficient in hydroxylysine and hydroxyproline and usually at least one commonly occurring amino acid and to have a high content of dicarboxylic acid and short chain amino acids and unreactive (blocked) NH2-terminal groups or aspartic acid-asparagine (Asx). However, the amyloid protein(s) from each individual differs from that of the others in molecular weight, in amino acid composition and in the presence or absence of specific tryptic peptides. Amyloid protein(s) from the liver and spleen of the same individual is identical. No chemical characteristics distinguish amyloid proteins derived from cases classified clinically as "primary" from those classified as "secondary." There is a striking chemical similarity between amyloid proteins and the NH2-terminal variable fragment of the light and heavy chain of immumoglobulin proteins.

scholarly journals MURINE AMYLOID FIBRIL PROTEIN: ISOLATION, PURIFICATION AND CHARACTERIZATION

1971 ◽  
Vol 19 (1) ◽  
pp. 16-28 ◽  
Author(s):  
G. G. GLENNER ◽  
D. PAGE ◽  
C. ISERSKY ◽  
M. HARADA ◽  
P. CUATRECASAS ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Structure Identification ◽  
Major Protein ◽  
Amyloid Protein ◽  
Molecular Weights ◽  
Sepharose 4B

Murine amyloid has been produced by four different induction methods ( Mycobacterium butyricum, casein, casein plus Freund's adjuvant and endotoxin-induced mouse amyloidosis) in several strains and obtained from mice with "spontaneous" amyloidosis. The amyloid fibrils have been concentrated from spleen and liver. Electron microscopy of all of these preparations reveals the amyloid fibril to be 100 Å in width and composed of two parallel filaments, each measuring 35-40 Å in width and having the appearance of a twisted ribbon. X-ray diffraction of all preparations reveals a "backbone" spacing at 4.75 Å and a "side chain" spacing at 11 Å indicating a "β-pleated sheet" structure. Identification of the major protein component of amyloid fibril concentrates was made by combined use of sodium dodecyl sulfate polyacrylamide disc electrophoresis, labeling of the protein with 3H-tryptophan and Sepharose 4B gel filtration. Purification of the amyloid protein from spontaneous amyloidosis liver was accomplished by sequential gel filtration with 5 M guanidine in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns. The material is a unique glycoprotein with a molecular weight of 7200, a high content of dicarboxylic and short chain amino acids, a significant amount of tryptophan and an unreactive NH2-terminal amino acid, tentatively identified as pyrrolid-2-one-5-carboxylic acid. There are no methionine, half-cystine, hydroxylysine or hydroxyproline residues. Murine amyloid protein, therefore, has striking similarities to many human amyloid protein preparations. It differs from the human proteins in the similarity of molecular weights of different preparations.

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

Axially Chiral Bis(α-amino Acid)s and Their Deamino Analogues. Synthesis and Configurational Assignment

1998 ◽  
Vol 63 (2) ◽  
pp. 211-221 ◽  
Author(s):  
Miloš Tichý ◽  
Luděk Ridvan ◽  
Miloš Buděšínský ◽  
Jiří Závada ◽  
Jaroslav Podlaha ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nmr Spectra ◽  
Building Blocks ◽  
X Ray Diffraction ◽  
Amino Groups ◽  
X Ray ◽  
Configurational Assignment ◽  
Symmetry Properties ◽  
Axially Chiral ◽  
Polymeric Structures

The axially chiral bis(α-amino acid)s cis-2 and trans-2 as possible building blocks for polymeric structures of novel type of helicity were prepared. Their configuration has been determined by NMR spectroscopy and, in the case of the trans-isomer, confirmed by single-crystal X-ray diffraction. Analogous pair of stereoisomeric diacids cis-3 and trans-3, devoid of the amino groups, was also prepared and their configuration assigned. The observed differences in the NMR spectra of cis- and trans-isomers of 2 and 3 are discussed from the viewpoint of their different symmetry properties.

scholarly journals Crystallization and preliminary X-ray diffraction analysis of UspE fromEscherichia coli

2014 ◽  
Vol 70 (12) ◽  
pp. 1640-1642 ◽  
Author(s):  
Yongbin Xu ◽  
Chun-Shan Quan ◽  
Xuanzhen Jin ◽  
Xiaoling Jin ◽  
Jing Zhao ◽  
...  
Keyword(s):  
Stress Proteins ◽  
Gel Filtration ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
Data Set ◽  
X Ray ◽  
Cell Parameters ◽  
E Coli ◽  
Vapour Diffusion ◽  
Induced Genes

Universal stress proteins (Usps) are among the most highly induced genes when bacteria are subjected to several stress conditions such as heat shock, nutrient starvation or the presence of oxidants or other stress agents.Escherichia colihas five small Usps and one tandem-type Usp. UspE (or YdaA) is the tandem-type Usp and consists of two Usp domains arranged in tandem. To date, the structure of UspE remains to be elucidated. To contribute to the molecular understanding of the function of the tandem-type UspE, UspE fromE. coliwas overexpressed and the recombinant protein was purified using Ni–NTA affinity, Q anion-exchange and gel-filtration chromatography. Crystals of UspE were obtained by sitting-drop vapour diffusion. A diffraction data set was collected to a resolution of 3.2 Å from flash-cooled crystals. The crystals belonged to the tetragonal space groupI4122 orI4322, with unit-cell parametersa=b= 121.1,c = 241.7 Å.

scholarly journals Synthesis, characterization, x-ray diffraction studies and biological activities of iron(III) and cobalt(II) complexes with alanine

2018 ◽  
Vol 6 (2) ◽  
pp. 132
Author(s):  
Shuaibu Musa ◽  
S O. Idris ◽  
A D. Onu
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Human Life ◽  
Molar Conductance ◽  
Biological Molecules ◽  
X Ray Diffraction ◽  
Monoclinic Crystal ◽  
X Ray ◽  
Metal Ligands ◽  
Elemental Analyses

The resulted complexes produced between Fe (III) and Co (II) with biological molecules like amino acids play an important role in human life. They can be used as bioactive compounds as well as in industries. Fe (III) and Co (II) complexes are synthesized with Alanine amino acid. The complexes were characterized by X-ray diffraction, magnetic suscetivility, elemental analysis (AAS), molar conductance, melting point, infrared and uv-visible spectrophotometry analyses. The elemental analyses were used to determine the chelation ratio, 1:3(metal: ligands) for iron (III) Alanine and 1:2 ratio for cobalt (II) Alanine. The molar conductivity of the complexes show that the complexes are not electrolytic in nature. The x-ray data suggest monoclinic crystal system for all the complexes with the exception of Co-alanine, which is hexagonal. The magnetic susceptivility and electronic spectra suggest the complexes are high spin with octahedral geometry.The complexes show enhance activity in comparable to the amino acid.  

Elucidation of the two-dimensional structure of an α-amino acid surfactant monolayer on water using synchrotron X-ray diffraction

Nature ◽  
1987 ◽  
Vol 328 (6125) ◽  
pp. 63-66 ◽  
Author(s):  
Sharon Grayer Wolf ◽  
Leslie Leiserowitz ◽  
Meir Lahav ◽  
Moshe Deutsch ◽  
Kristian Kjaer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray

scholarly journals Clay intercalated Cu(II) amino acid complexes: synthesis, spectroscopy and catalysis

Clay Minerals ◽  
1996 ◽  
Vol 31 (4) ◽  
pp. 491-500 ◽  
Author(s):  
L. Fu ◽  
B. M. Weckhuysen ◽  
A. A. Verberckmoes ◽  
R. A. Schoonheydt
Keyword(s):  
Amino Acid ◽  
Diffuse Reflectance ◽  
Diffuse Reflectance Spectroscopy ◽  
The Novel ◽  
Oxidation Reactions ◽  
Axially Symmetric ◽  
X Ray Diffraction ◽  
X Ray ◽  
Spin Resonance ◽  
Synthesized Materials

AbstractComplexes of Cu(lysine)2+2 and Cu(histidine)2+2 have been intercalated between the layers of saponite clays by a simple cation exchange procedure from aqueous solutions of preformed Cu(amino acid)2-complexes. Successful immobilization was obtained with an amino acid: Cu2+ ratio of 5, and a pH of 10 and 7.3 for lysine and histidine, respectively. The synthesized materials were investigated as powders and as thin films by electron spin resonance (ESR), diffuse reflectance spectroscopy (DRS) and X-ray diffraction (XRD). The light blue clays are characterized by an axially symmetric ESR spectrum with A//= 192 G, g//= 2.23 and g⊥ = 2.07, and a d-d absorption band around 600 nm, due to the intercalated planar Cu2+-complexes. Ammonia interacts reversibly with these intercalated complexes, suggesting the presence of a free coordination site. The novel synthesized materials are active in various oxidation reactions with t-butyl hydroperoxide as oxidant.

Metallkomplexe mit biologisch wichtigen Liganden, CXV. Addition von α-Aminosäureestern an [CpFe(CO)3]+: Carbamoylkomplexe Cp(OC)2Fe-C(O)NHCHRCO2R’ und Kristallstruktur von Cp(OC)2Fe-C(O)NHCH2CO2Et / Metal Complexes of Biologically Important Ligands, CXV. Addition of α-Amino Acid Esters to [CpFe(CO)3]+: Carbamoyl Complexes Cp(OC)2Fe-C(O)NHCHRCO2R' and Crystal Structure of Cp(OC)2Fe-C(O)NHCH2CO2Et

1999 ◽  
Vol 54 (3) ◽  
pp. 385-388 ◽  
Author(s):  
Reinhold Urban ◽  
Kurt Polbom ◽  
Wolfgang Beck
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Metal Complexes ◽  
Amino Acid Esters ◽  
X Ray Diffraction ◽  
Carbonyl Ligand ◽  
X Ray ◽  
Acid Esters

α-Amino acid esters can be added to a carbonyl ligand of [CpFe(CO)3]+CF3SO3- to give the carbamoyl complexes Cp(OC)2Fe-C(O)NHCHRCO2R′ (R = H, Me, CHMe2, CH2Ph; R′ = Et, Me). This type of reaction may be useful for the marking of peptides at the amino end. The crystal structure of Cp(OC)2Fe-C(O)NHCH2CO2Et was determined by X-ray diffraction.

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