Ontogenetic trends in aspartic acid racemization and amino acid composition within modern and fossil shells of the bivalve Arctica

2001 ◽  
Vol 65 (12) ◽  
pp. 1921-1932 ◽  
Author(s):  
Glenn A Goodfriend ◽  
Christopher R Weidman
1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.


Author(s):  
A. I. Fedosov ◽  
V. S. Kyslychenko ◽  
O. M. Novosel

Introduction. Plant amino acids have an important impact on functioning of various systems and organs of human body. In addition, they possess a wide range of pharmacotherapeutic properties, improve the digestion and potentiate the activity of biologically active compounds present in plants. Thus, the search of plant species that contain a large complex of plant amino acids and are used as food is of current interest. Garlic (Allium sativum L.) from Alliaceae family is one of such plants, and has been used since ancient times for the treatment of various disorders.The aim of the study – to determine the composition and quantitative content of free and bound amino acids of garlic bulbs and leaves.Research methods. The amino acid composition was determined using the high-performance liquid chromatography (HPLC) method.Results and Discussion. 16 amino acids were detected in garlic bulbs as a result of the experiment. Arginine (3.04 %) and proline (1.56 %) were found to be accumulated infree state, while glutamic acid (10.59 %), aspartic acid (6.06 %) and arginine (5.94 %) prevailed in bound state. 15 free and 16 bound amino acids were identified and quantified in garlic leaves. Glutamic acid (2.11 %), leucine (1.79 %), valine (1.77 %), isoleucine (1.52 %), treonine and phenylalanine (1.44 %) dominated infree state, and glutamic acid (28.49 %), aspartic acid (12.90 %) and leucine (7.61 %) prevailed in bound state. Methionine was found only in bound state in garlic leaves.Conclusions. The amino acid composition of garlic bulbs and leaves was studied using the HPLC method. 16 amino acids in both free and bound state were detected and their content was determined in garlic bulbs, while in garlic leaves – 15 free and 16 bound amino acids. The results of the experiment showed that methionine is present only in bound state in garlic leaves.


Biosystems ◽  
1986 ◽  
Vol 19 (4) ◽  
pp. 267-272 ◽  
Author(s):  
Manuel Martínez Luque-Romero ◽  
Luis Sánchez de Medina ◽  
Juan Muñoz Blanco

1972 ◽  
Vol 78 (2) ◽  
pp. 265-273 ◽  
Author(s):  
D. B. Smith

SUMMARYThe amino acid composition of barley grain was studied during the maturation of the grain and during germination of the mature grain. Samples of the variety Proctor, grown at two nitrogen levels in each of the years 1969 and 1970, were analysed together with one sample of Sultan grown in 1970. It was found that during maturation the proportions of glutamic acid and proline increased and that the levels of these amino acids were highest in those samples with the highest total protein content. During ripening the proportions of lysine, alanine, aspartic acid, threonine and glycine decreased. On germination the proportions of glutamic acid and proline rapidly decreased whilst aspartic acid, lysine, alanine and glycine increased.The nutritive value of ripe barley grain is limited by its low lysine content. Whilst the germination process increases the level of lysine it is suggested that this does not increase the nutritional value of the grain due to the low level of cystine in the germinated grain.


1969 ◽  
Vol 112 (1) ◽  
pp. 41-49 ◽  
Author(s):  
J. M. Gillespie ◽  
Andrea Broad ◽  
P. J. Reis

When the diet of sheep is supplemented by the infusion of sulphur-containing amino acids or casein into the abomasum, the newly synthesized wool shows characteristic changes in its amino acid composition, with significant increases in cystine, proline and serine and decreases in aspartic acid and phenylalanine. This modification seems to be due entirely to an alteration in the overall composition of the high-sulphur proteins and to an increase in their proportion in the fibre. These variations are not the result of a change in the composition of individual proteins, but are due to alterations in their relative proportions and to the initiation of the synthesis of ‘new’ proteins, many of which are extremely rich in cystine. It is suggested that the heterogeneity of the high-sulphur proteins may be due, in part, to similar changes in composition caused by natural variations in the nutrition of sheep.


1942 ◽  
Vol 15 (1) ◽  
pp. 96-106
Author(s):  
G. S. Whitby ◽  
H. Greenberg

Abstract The following amino acids are shown to occur in the serum of the latex of Hevea brasiliensis, all except the last having been actually isolated from it: tyrosine, l-leucine, d-iso-leucine, d-valine, d-arginine, l-aspartic acid, i-proline, and phenylalanine. A cursory examination of the amino-acid composition of the heat-coagulable protein of latex has been made. A tabular summary is given of the results obtained by various workers to date on the amino-acid composition of latex and latex proteins.


1965 ◽  
Vol 11 (4) ◽  
pp. 605-610 ◽  
Author(s):  
E. A. Grula ◽  
Gerald L. Smith ◽  
Mary M. Grula

The Erwinia sp. studied possesses a discrete mucopeptide layer. This layer contains glutamic, diaminopimelic, and muramic acid, glucosamine, and alanine (1–1–1–1–2) as major components. Aspartic acid, glycine, and an unidentified ninhydrin-positive compound are also present but in lesser amounts. Content of glycine increases when cells are grown in a defined medium in the presence of glycine. Serine is present in the mucopeptide when cells are grown in the presence of D-serine, an inhibitor of cell division. Serine can partially replace glycine. Incorporation of serine is not significantly decreased by agents capable of preventing division inhibition by D-serine (pantoyl lactone or ammonium chloride). A new method for isolation of pure mucopeptide is presented.


1980 ◽  
Vol 45 (7) ◽  
pp. 2131-2134 ◽  
Author(s):  
Helena Keilová ◽  
Vladimír Kostka ◽  
Miroslav Baudyš

A peptide was isolated from chicken pepsin which contains the aspartic acid residue reacting with diazoacetyl-D,L-norleucine methyl ester in the presence of Cu2+ -ions. The peptide is N-terminated with isoleucine and contains (besides isoleucine) valine, aspartic acid, two threonines, serine, and leucine. In concurrent experiments a peptide of the same composition was isolated from the thermolysin digest of chicken pepsin and its sequence determined as Ile-Val-Asp-Thr-Gly-Thr-Ser-Leu. Since both peptides have entirely identical amino acid composition and other characteristics, the sequenced peptide corresponds to the peptide isolated from the active site of the enzyme.


1955 ◽  
Vol 8 (1) ◽  
pp. 114 ◽  
Author(s):  
DH Simmonds

The amino acid composition of a protein component of Merino 64's quality wool, which moves as a single peak on electrophoresis in alkaline thioglycollate solutions, has been determined. The results, which are summarized in Table 1, show that the purified protein fraction contains more aspartic acid, glutamic acid, leucine, lysine, and amide nitrogen, and less cystine, proline, serine, and tryptophan, than the parent wool from which it was extracted.


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