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.

SAFETY OF PRODUCTS OF SLAUGHTER GALEENY IN APPLICATION OF PROTEIN HYDROLYSATES

2019 ◽  
Vol 1 (2) ◽  
pp. 126-131
Author(s):  
V. M. Bachinskaya ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Nitrogen Retention ◽  
Protein Hydrolysates ◽  
The Body ◽  
Biological Value ◽  
Poultry Products ◽  
Protein Components

The quality and safety of poultry products for consumers is one of the main indicators. The concept of «quality of food» includes indicators of usefulness (nutritional and biological value), good quality and harmlessness. The biological value of the product is determined by the quality of protein components, their amino acid composition and expressed by the degree of nitrogen retention of food in the body of growing animals [1]. This article presents materials on the study of the effect of Abiopeptid and Ferropeptid protein hydrolysates on the amino acid composition of meat, the content of macro- and microelements in it, the relative biological value of meat, and also on safety indicators.

scholarly journals Studies on Chitin IV. The Occurrence of Complexes in Which Chitin and Protein are Covalently Linked

1960 ◽  
Vol 13 (4) ◽  
pp. 568 ◽  
Author(s):  
RH Hackman
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Covalent Bonds ◽  
Protein Components ◽  
Covalently Linked ◽  
Different Sources

Samples of chitin have been prepared from the cuticles of insects and crustacea, from cuttlefish shell, and from the skeletal pen of squid. In every case protein was bound by covalent bonds to the chitin so forming stable complexes (glycoproteins). Glycoproteins from different sources contained differing amounts of chitin and protein, the ratio of chitin to protein varying from 1 : 1 to 20 : 1. The protein would appear to be linked to the chitin through aspartyl or histidyl residues or both and each glycoprotein is polydisperse. The chitin preparations included glycoproteins which contained a;- and {3-type chitina and also a third and different type of chitin. The amino acid composition of the protein components of the glycoproteins has been determined. It ia probable that chitin does not occur uncombined with protein.

scholarly journals Studies on Reduced Wool V. A Comparison of the Two Major Components

1965 ◽  
Vol 18 (6) ◽  
pp. 1207 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Deae Cellulose ◽  
Major Protein ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Protein Components ◽  
Wool Proteins ◽  
Peptide Maps

Starch-gel electrophoresis of wool proteins extracted from reduced and carboxymethylated wool gives a complex pattern in which there are two major protein bands. By a combination of chromatography on DEAE-cellulose and gelfiltration in buffers containing 8M urea these two protein components have been isolated. The amino acid composition and some properties of these two fractions are reported. A comparison of the amino acid composition and of peptide maps of tryptic digests of the two fractions shows distinct differences between them, and by labelling with 2-[14C]iodoacetate the distribution of the peptides containing S-carboxymethylcysteine residues were also shown to be different.

Amino acid composition of gluten fractions

1969 ◽  
Vol 47 (3) ◽  
pp. 379-390
Author(s):  
Haung-Ju Yang ◽  
A. G. McCalla
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Disulfide Bonds ◽  
Sodium Salicylate ◽  
Sodium Sulfite ◽  
Dispersing Agent ◽  
Protein Components ◽  
Hydrolysis Of ◽  
Soluble Fractions

Gluten dispersions in 10% sodium salicylate were fractionated by precipitation with increasing concentrations of magnesium sulfate. Dialysis of the dispersion against the dispersing agent to which sodium bisulfite had been added served merely to sharpen the separation of the fractions. Dialysis against the dispersing agent to which sodium sulfite had been added resulted in failure to recover much of the less soluble portion of the gluten by precipitation. It is suggested that the sulfite ruptured disulfide bonds of the less soluble fractions of gluten.The amino acid composition of successive fractions varied regularly, with the less soluble fractions containing less glutamic acid and proline and more arginine, lysine, aspartic acid, threonine, glycine, alanine, and tryptophan than did the more soluble fractions. This relationship among fractions was not altered by the exposure of gluten to reducing agents.Precipitates produced during hydrolysis of the gluten fractions by papain also varied regularly in amino acid composition but the proportions of individual amino acids were entirely different from those for the total protein in the fraction.Gluten must be considered as a complex combination of protein components but the number of components involved cannot yet be determined.

scholarly journals Affinity-chromatographic isolation and some properties of troponin C from different muscle types

1977 ◽  
Vol 161 (3) ◽  
pp. 465-471 ◽  
Author(s):  
J F Head ◽  
R A Weeks ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Troponin I ◽  
Smooth Muscles ◽  
Troponin C ◽  
Electrophoretic Mobilities ◽  
Muscle Types ◽  
Chromatographic Isolation

1. The formation of a complex between troponin I and troponin C that is stable in 6M-urea and dependent on Ca2+ was demonstrated in extracts of vertebrate striated and smooth muscles. 2. A method using troponin I coupled to Sepharose is described for the rapid isolation of troponin C from striated and smooth muscles of vertebrates. 3. Troponin C of rabbit cardiac muscle differs significantly in amino acid composition from troponin C of skeletal muscle. The primary structures of troponin C of red and white skeletal muscle are very similar. 4. The troponin C-like protein isolated from rabbit uterus muscle has a slightly different amino acid composition, but possess many similar properties to the forms of troponin C isolated from other muscle types. 5. The electrophoretic mobilities of the I-troponin C complexes formed from components isolated from different muscle types are determined by the troponin I component.

Isoloation of H-SF substances, the high-molecular-weight precursors of egg envelope preteins, from the ascites accumulated in the oestrogen-treated fish Oryzias latipes

Zygote ◽  
1993 ◽  
Vol 1 (4) ◽  
pp. 315-324 ◽  
Author(s):  
Kenji Murata ◽  
Ichiro Iuchi ◽  
Kenjiro Yamagami
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Oryzias Latipes ◽  
Prolonged Treatment ◽  
Egg Envelope ◽  
Molecular Weights ◽  
Female Specific ◽  
Whole Egg

High- and low-molecular weight spawning-female-specific (H-SF and L-SF) substances are liver-derived putative precursors of the inner layer of egg envelope of the medaka Oryzias latipes, and are also found in the ascites which are accumulated in the male fish on prolonged treatment with oestrogen. In the present study, the H-SF substances purified from the ascites of the oestrogen-treated male medaka were found to consist of three proteins. Their molecular weights ranged from 74 000 to 76 000, which corresponds to those of ZI-1 and ZI-2, the major components of medaka egg envelope. The amino acid composition of the H-SF substances was characterised by high contents of proline (17.58 mol%) and glutamic acid/glutamine (13.34 mol%). The characteristics were almost identical to those of ZI-1 and ZI-2 but differed from those of L-SF substance, a precursor of ZI-3, another major component of the egg envelope. These results confirm our view that H-SF substances are the precursors of ZI-1 and ZI-2. The average amino acid compositions of H-SF substances and L-SF subsatance coincided with the amino acid composition of whole egg envelope. This result strongly suggests that an equal amount of H-SF substances and L-SF substance would construct the inner layer of egg envelope after a little modification.

Occurrence of the Bacteriochlorophyll-Binding Polypeptides B870α and B800— B850α in the Mutant Strains Y5 and Ala+ of Rhodopseudomonas capsulata, which are Defective in Formation of the Light-Harvesting Complexes B870 and B800 — 850, Respectively

1984 ◽  
Vol 39 (9-10) ◽  
pp. 922-926 ◽  
Author(s):  
Monier H. Tadros ◽  
Roland Dierstein ◽  
Gerhart Drews
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Light Harvesting ◽  
Rhodopseudomonas Capsulata ◽  
Terminal Sequence ◽  
Light Harvesting Complexes ◽  
Mutant Strains ◽  
Protein Components

Abstract The mutant strains A l a+ and Y 5 of Rhodopseudomonas capsulata are defective in formation of the light-harvesting complexes B800-850 and B870, respectively, but synthesize the large bacteriochlorophyll-binding polypeptides of the respectively complexes, shown by amino acid composition, N- or C-terminal sequence and immunoblotting. The stable assembly of the light-harvesting complexes in the membrane seems to be dependent from the coordinated synthesis of all pigment and protein components.

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