scholarly journals Calmodulin is a major component of extruded trichocysts from Paramecium tetraurelia.

1981 ◽  
Vol 91 (3) ◽  
pp. 860-865 ◽  
Author(s):  
J J Rauh ◽  
D L Nelson
Keyword(s):  
Heat Treatment ◽  
Amino Acid ◽  
Affinity Chromatography ◽  
Amino Acid Composition ◽  
The Other ◽  
Paramecium Tetraurelia ◽  
Whole Cells ◽  
Molecular Weights ◽  
Heat Stable ◽  
Composition Characteristic

Extruded trichocysts are composed of a family of proteins with molecular weights between 15,000 and 20,000. We have used heat treatment and affinity chromatography on fluphenazine-Sepharose to purify calmodulinlike proteins from whole cells and from extruded trichocysts. The purified protein from trichocysts is indistinguishable from that of whole cells; it is heat-stable, activates brain phosphodiesterase in a Ca++-dependent fashion, changes mobility on SDS polyacrylamide gels in the presence of Ca++, contains 1 mol of trimethyllysine/17 kdaltons, and has the amino acid composition characteristic of calmodulins. Calmodulin is a major component of purified, extruded trichocysts, of which it represents between 1 and 10% by mass. The other proteins of the trichocyst also resemble calmodulin in several properties. Possible roles for calmodulin in the Ca++-activated extrusion of trichocysts is discussed.

scholarly journals Cationic Proteins of Human Granulocytes. II. Separation of the Cationic Proteins of the Granules of Leukemic Myeloid Cells

Blood ◽  
1974 ◽  
Vol 44 (2) ◽  
pp. 235-246 ◽  
Author(s):  
I. Olsson ◽  
P. Venge
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Aminocaproic Acid ◽  
Cationic Protein ◽  
Cationic Proteins ◽  
Molecular Weights ◽  
Electrophoretic Mobilities ◽  
Human Granulocytes ◽  
Protein Components

Abstract The highly cationic proteins of human granulocytes, whose electrophoretic mobilities toward the cathode are faster than that for lysozyme, were isolated from the cytoplasmic granules of leukocytes, obtained from patients with chronic myeloid leukemia. The granule extract was subjected to chromatography on Sephadex G-75 and E-aminocaproic acid-Sepharose ion adsorbant followed by preparative electrophoresis on agarose. Seven cationic protein components were identified, and five of these were obtained in a pure form. One group of cationic proteins, including components 1-4, exhibited molecular weights in the range 25,500-28,500, almost identical amino acid composition, and complete immunologic identity. Another group of proteins, including components 5-7, exhibited molecular weights in the range 21,000-29,000 and also showed complete immunologic identity; amino acid analysis performed on component 5 indicated a different amino acid composition from that of components 1-4. Cationic proteins with similar electrophoretic mobilities and immunochemical identities were also detected in granule extracts of granulocytes from healthy individuals. The proteins isolated from human granulocytes have a higher molecular weight and a lower content of basic amino acids than the cationic proteins with antibacterial and permeability-increasing properties previously demonstrated in rabbit polymorphonuclear granulocytes.

Proteins in the Enamel Fluid of Immature Porcine Teeth

1987 ◽  
Vol 66 (12) ◽  
pp. 1721-1726 ◽  
Author(s):  
T. Aoba ◽  
T. Tanabe ◽  
E.C. Moreno
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Content ◽  
Acid Composition ◽  
Permanent Teeth ◽  
Major Protein ◽  
Protein Species ◽  
Terminal Sequence ◽  
Molecular Weights ◽  
Sds Electrophoresis

The fluid was separated from the immature soft enamel of porcine permanent teeth in the secretory stage according to procedures reported previously (Aoba and Moreno, 1987). The protein content of the fluid was about 2.8% w/v; its amino-acid composition was characterized by high contents of Pro, Glx, Leu, and His, showing composition similar to that of the 20 kilo-dalton (kd) amelogenin or its C-terminal segments. The two major protein species in the fluid had apparent molecular weights of 13 kd and 11 kd, as determined by SDS electrophoresis; the N-terminal residue of the former was Leu, while that of the latter was Ala. The C-terminal sequence of both of them was -Met-Phe-Ser. By comparison with the published sequence of 20-kd porcine amelogenin, it is concluded that the main fluid constituents were derived by cleavages of N-terminal segments from the 20-kd amelogenin.

NATURE OF PROTEINS IN TRITICALE AND ITS PARENTAL SPECIES: I. SOLUBILITY CHARACTERISTICS AND AMINO ACID COMPOSITION OF ENDOSPERM PROTEINS

1970 ◽  
Vol 50 (1) ◽  
pp. 9-14 ◽  
Author(s):  
C. H. CHEN ◽  
W. BUSHUK
Keyword(s):  
Amino Acid ◽  
Durum Wheat ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Spring Wheat ◽  
Water Soluble ◽  
The Other ◽  
Hard Red Spring Wheat ◽  
Endosperm Proteins ◽  
Spring Wheat Cultivar

Solubility characteristics and amino acid composition of the endosperm proteins of one line of Triticale, its durum wheat and rye parent cultivars, and one cultivar of hard red spring wheat were compared. Quantitative distribution of the soluble protein fractions and amino acid compositions showed that the proteins of Triticale are intermediate in these properties between analogous properties of the proteins of its durum wheat and rye parents. The major differences between the hard red spring wheat and the other three species were its lower content of water-soluble proteins and higher content of insoluble or gluten proteins. This appears lo be the main reason for the superior breadmaking quality of the hard red spring wheat cultivar compared with the other species used in this study.

OXYTOCIN AS A NEUROHYPOPHYSIAL HORMONE IN THE HOLOCEPHALIAN ELASMOBRANCH FISH, HYDROLAGUS COLLEI

1969 ◽  
Vol 45 (4) ◽  
pp. 597-606 ◽  
Author(s):  
B. T. PICKERING ◽  
H. HELLER
Keyword(s):  
Amino Acid ◽  
Pituitary Gland ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
The Other ◽  
Pharmacological Properties ◽  
Neurohypophysial Hormones ◽  
Elasmobranch Fish

SUMMARY Two peptides with uterotonic activity have been isolated from the pituitary gland of a holocephalian elasmobranch fish: Hydrolagus collei. One of them had an amino acid composition compatible with that of oxytocin itself, and also had the pharmacological properties of this hormone. The other peptide which was present in much smaller amounts was basic by chromatography and had the pharmacological characteristics of [8-arginine]-oxytocin. It was not completely purified because of the small amount available, but its amino acid composition was in accord with that of vasotocin. The implications of the presence of oxytocin in such a primitive fish on the phylogeny, and hence probably the evolution, of neurohypophysial hormones are discussed.

scholarly journals Studies on the subunits of human myeloperoxidase

1984 ◽  
Vol 222 (3) ◽  
pp. 701-709 ◽  
Author(s):  
R L Olsen ◽  
C Little
Keyword(s):  
Heat Treatment ◽  
Amino Acid ◽  
Molecular Mass ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Additional Species ◽  
Main Protein

The subunit composition of human myeloperoxidase was studied with the use of sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and gel filtration. The subunit pattern observed depended on the manner in which the enzyme was treated before analysis. Reduction before heat treatment in detergent led to two main protein species (Mr 57 000 and 10 500), whereas reduction during or after heat treatment yielded an additional species of Mr 39 000. Heating without any reductive pretreatment yielded the 39 000-Mr form as the major electrophoretic species. Carbohydrate staining showed large amounts of sugar on the 57 000-Mr species and little on the 10 500-Mr form. Significant amounts of haem were associated with this latter subunit. Haem also seemed to be associated with the 57 000-Mr form but not with the 39 000-Mr one. These three subunit forms were isolated and their amino acid composition analysed. The 57 000-Mr and 39 000-Mr forms had very similar amino acid composition and yielded an apparently identical collection of fragments on incubation with CNBr. Once separated, the subunits could not be interconverted. Generally, minor amounts of other molecular-mass forms were observed. The nature of the various molecular-mass forms originating from myeloperoxidase is discussed.

Isolation and Properties of Elastase-Like Enzymes from Human Platelets and Pig Aorta

1975 ◽  
Author(s):  
W. Hornebeck ◽  
Y. Legrand ◽  
J. P. Caen ◽  
L. Robert
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Affinity Chromatography ◽  
Amino Acid Composition ◽  
Proteolytic Activity ◽  
Gel Filtration ◽  
Inhibitory Effect ◽  
Human Platelets ◽  
Purification Procedure ◽  
Pancreatic Elastase

An elastase-like enzyme has been isolated from human platelets. Its purification using precipitations with ammonium sulphate, gel filtration and affinity chromatography on Agarose-elastin, is described. The acrylamide gel of the affinity peak reveals only one band corresponding to a molecular weight of about 25,000 daltons. The amino acid composition is similar to pancreatic elastase. Using the same kind of purification procedure an aortic elastase-like enzyme has also been isolated and characterized. These two enzymes possess comparable proteolytic activity on various synthetic and natural substrates considered as specific for elastases. The ratio of their activity on these substrates differs however from that of pancreatic elastase. The inhibitory effect of α1, antitrypsine and α2 macroglobuline were also studied and shown to differ quantitatively from those on pancreatic elastase. These elastase like enzymes may be responsible for the degradation of elastin occuring in ageing and arteriosclerosis.

Effect of heat treatment on amino acid composition of canned baby food

1978 ◽  
Vol 26 (3) ◽  
pp. 766-768 ◽  
Author(s):  
Raimo P. Raunio ◽  
Pirjo S. Alho ◽  
Reino R. Linko
Keyword(s):  
Heat Treatment ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Baby Food

ORGANIC NITROGEN DISTRIBUTION IN SELECTED PEATS AND PEAT FRACTIONS

1978 ◽  
Vol 58 (2) ◽  
pp. 237-249 ◽  
Author(s):  
F. J. SOWDEN ◽  
H. MORITA ◽  
M. LEVESQUE
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Acid Amide ◽  
Amino Sugar ◽  
The Other ◽  
Total N ◽  
Mesh Material ◽  
The Individual

The nitrogenous products formed by 6 N HCl hydrolysis of a variety of peats including a cultivated mesic profile, a virgin humic profile, a sedge, a woody and a sphagnum fibric peat were studied. Peat fractions separated according to particle size, woody and herbaceous materials isolated from a peat sample, and Typha and Carex plants growing on peat soils were also analyzed. Of the two profiles examined, the cultivated mesic peat showed significant quantitative changes in the content of individual amino acids throughout the profile. Also the amino sugar and amino acid N increased to a maximum, then decreased. On the other hand, the virgin humic peat profile exhibited random variations in the content of the individual amino acids and in the amount of amino acid N. Of the other peats examined, the fibric sphagnum had the highest percentage of amino acid N. Among the separates, the 100- to 200-mesh material had the highest proportion of amino acid N. The amino acid composition of the plant remains from the peat was similar to that of the peat from which it was isolated. The amino acid composition of the Typha and Carex plants was different from that of peat in that 75% of their total N content could be accounted for on the basis of amino acid, amide and amino sugar N. The amounts of hydroxyproline and the amino sugars in peats vary more than that of the amino compounds. In contrast to inorganic soils, which tend to have a similar amino acid composition, these limited data suggest that the amino acid and amino sugar contents of peats may be characteristic of individual bogs.

Amino acid composition of casein isolated from the milks of different species

1977 ◽  
Vol 55 (1) ◽  
pp. 231-236 ◽  
Author(s):  
Bruce H. Lauer ◽  
Bruce E. Baker
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Hydrolysis ◽  
Acid Composition ◽  
Chromatographic Analysis ◽  
Polar Bear ◽  
The Other ◽  
Fin Whale ◽  
Musk Ox

Casein was isolated from the milks of the following species: cow, horse, pig, reindeer, caribou, moose, harp seal, musk-ox, polar bear, dall sheep, and fin whale. The caseins were subjected to acid hydrolysis, the resultant amino acids were converted to their n-butyl-N-trifluoroacetyl esters, and the amino acid composition of the caseins was determined by gas chromatographic analysis of these esters. Notable among the results was the close similarity, with respect to amino acid composition, of reindeer and caribou caseins. The results of the amino acid analyses of the other caseins are presented and discussed.

scholarly journals pIPredict Version 2: New Features and PTM Analysis

2018 ◽  
Vol 1 (2) ◽  
pp. e00009 ◽  
Author(s):  
V.S. Skvortsov ◽  
N.N. Alekseychuk ◽  
Yu.V. Miroshnichenko ◽  
A.V. Rybina
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Isoelectric Point ◽  
The Other ◽  
2D Electrophoresis ◽  
Chemical Modifications ◽  
Post Translational Modifications ◽  
Pka Values ◽  
Java Application

pIPredict was created as a tool for prediction of the isoelectric point of peptides and proteins. It can also generate virtual 2D electrophoresis maps. The method of pI prediction is based on the Henderson-Hasselbach equation. In a new version the ProMoST and our new scales of pKa values were added. The other added features included: correction of electrophoretic shift by analyzing amino acid composition of proteins and prediction of pI values for proteins with a new set of posttranslational and other chemical modifications. Prediction of pI for proteins with PTM can be used to predict position of modified proteoforms on the virtual 2D electrophoresis map or as the tool of identifying which particular proteoform was observed in the experiment.The program also includes several widely used pKa scales, that can partially calculate values for proteins with some post-translational modifications. pIPredict is created as JAVA application and is freely available at http://www.ibmc.msk.ru/LPCIT/pIPredict.

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