scholarly journals On the Nutrition and Metabolism of Zooplankton II. The relationship between the marine copepod Calanus helgolandicus and particulate material in Plymouth sea water, in terms of amino acid composition

Author(s):  
C. B. Cowey ◽  
E. D. S. Corner

The amino acid composition of adult female Calanus helgolandicus Claus and particulate material at station L4 has been analysed from March to December. The average concentration of amino acid nitrogen in Calanus was 7·7% of the dry body weight and accounted for 83% of the total nitrogen. The average level of amino acid nitrogen in the particulate material was 11·9 μg/1. and accounted for 54% of the total nitrogen.The relative quantities of amino acids in Calanus remained remarkably constant throughout the year. The relative quantities of amino acids in particulate material were more variable.The rate of respiration of Calanus measured at 8°C varied from 31 μl. O2/mg. dry body weight/day in winter (December–February) to 79 μl. O2/mg dry body weight/day in summer (April–August).Starving winter Calanus lost 1·8% and starving summer Calanus 2·1% of their dry body weight as amino acids each day. In order to replenish its daily losses of amino acids winter Calanus must sustain a filtering rate of about 30 ml./animal/day: the corresponding value in summer is greater than 50 ml./animal/day.The amino acid composition of Skeletonema costatum is so close to that of the particulate material in the sea, that, as far as amino acids are concerned, Calanus would gain no nutritional advantage by selecting the diatom in preference to the amino acid containing fraction of particulate material as a whole.

1977 ◽  
Vol 57 (4) ◽  
pp. 445-456 ◽  
Author(s):  
F. J. SOWDEN

Forms of nitrogen in 92 samples were measured in a study designed to determine the similarities and differences in the nitrogen distribution in various horizons of a wide range of Canadian soils. The samples, representing all of the nine soil orders, were chosen from different climate and vegetation zones. Some peat soils were analyzed also. The data were first grouped according to the nitrogen content of the samples, but the amino acid composition of the soil "protein" did not appear to be related to this. The data were then grouped according to LFH, A, B and C horizons and also according to the Ah, Ap, Ae, Bhf, Bh, Bm and Bt layers. Again, few significant differences in the amino acid composition could be found. Data for the average amino acid composition and standard deviations for 92 mineral soils, 6 LFH and 2 ’O’ horizons of these and 18 peat soils were calculated. Since the analytical and sampling errors appear to be relatively small and would not account for all the variation between samples, there appeared to be real but relatively small and random differences in the amino acid composition of the different samples. The data for the individual soils supported this conclusion; for instance, some samples had very small or barely detectable amounts of hydroxyproline, while with other soils it made up 1–2% of the amino acid nitrogen. The amino sugar composition was more variable and the glucosamine/galactosamine ratio varied from 2:1 for the LFH horizons to 1:1 for the peat soils. In general, however, the soil "protein", which is probably largely the result of microbial degradation and synthesis, is remarkably similar to its amino acid composition. Amino acid nitrogen made up over half of the total nitrogen of the LFH and O horizons. This underestimated the "protein" nitrogen, since there is probably some amide nitrogen (about 5%) not included. In the mineral soils probably about 40% was "protein" nitrogen (including aminde), 5% was amino sugar nitrogen, 18% hydrolyzable unidentified nitrogen and 13.5% was insoluble in the acid used for hydrolysis. Clay-fixed ammonium made up 17% of the total nitrogen and much of the hydrolyzable ammonium came from this.


1998 ◽  
Vol 67 (1) ◽  
pp. 165-170 ◽  
Author(s):  
W. H. Hendriks ◽  
M. F. Tarttelin ◽  
P. J. Moughan

AbstractThe amino acid composition of cat hair was determined by conventional 24-h acid hydrolysis and non-linear least-squares extrapolation to time zero of the amino acid composition data from a series of hydrolysis intervals. Twenty-five individual samples of cat hair, consisting of four colours, were also analysed (24-h hydrolysis) to determine if there was an effect of hair colour on amino acid composition. Amino acids were determined following HCl hydrolysis (6 mol/l) with cysteine and methionine determined by performic acid oxidation of the sample prior to hydrolysis.There was no significant (P > 0·05) effect of hair colour on the amino acid composition of cat hair. The non-linear compartmental model used to determine the amino acid composition of cat hair took into account the simultaneously occurring processes of hydrolysis and degradation of amino acids over time. The amino acids cysteic acid, methionine-sulphone, threonine and serine exhibited high loss rates during 6 molll HCl hydrolysis while the peptide bonds involving valine and leucine were slowly hydrolysed. Amino acid nitrogen accounted for 0·94 of the total nitrogen in cat hair when determined by conventional 24-h hydrolysis and 0·99 of the total nitrogen when the compartmental model was applied. The average nitrogen proportion in cat hair protein was found to be 0·175. The amino acid composition of cat hair protein is comparable with that of dog, horse, sheep and human hair although the proline content of cat hair protein appears to be lower than that in the other species.


1993 ◽  
Vol 120 (1) ◽  
pp. 129-133 ◽  
Author(s):  
R. J. Wallace ◽  
C. J. Newbold ◽  
N. D. Watt ◽  
V. Buchan ◽  
D. S. Brown

SUMMARYRumen fluid was removed from four sheep 6 h after feeding, and the fluid was centrifuged to remove the micro-organisms. Perchloric acid (PCA) was added to the supernatant fluid to precipitate soluble proteins, which were again removed by centrifugation. The PCA extract was neutralized with KOH and the precipitate was removed by centrifugation. The supernatant fluid was hydrolysed with 6 MHC1 at 110 °C for 24 h, then dried by rotary evaporation, and the amino acid composition of each extract was analysed by ion-exchange chromatography. The recovery of amino acids was 98%, except for methionine, cysteine and tryptophan, which were destroyed. The recovery of amino acids from added Trypticase was 92% of the peptide mixture as amino acids. The free amino acid composition of extracellular rumen fluid was low and variable in both amount and composition (0·36, S.D. 0·49, μmol/ml). The concentration of amino acids released by acid hydrolysis of the PCA extract, presumed to be derived from peptides, was larger and its composition was less variable (1 ·02, S.D. 0·30, μmol/ml). Aspartic acid and histidine were enriched in peptides in comparison with the amino acids present in the feed or in rumen particulate material. Glycine and proline contents were higher in peptides that in particulate material. In contrast, the contents of isoleucine, leucine, tyrosine and phenylalanine tended to be lower in peptides than in the other materials. It was concluded that extracellular degradation-resistant peptides had a composition that was different to microbial protein and to the feed. The peptides appeared to be enriched for amino acids which previous studies with pure peptides had shown tend to make peptides more resistant to degradation.


2013 ◽  
Vol 41 (1) ◽  
pp. 69-75
Author(s):  
Ryszard Kosson

The contribution of cotyledons, embryo and testa to the whole seed, was analyzed in the bean cultivar, Wiejska. The total nitrogen content and amino acid composition of morphological parts of the seed were determined. The average amino acid composition of globulins and albumins and the content of free amino acids in seeds of six Polish cultivars were estimated as well. It was found that the embryo contained the highest quantity of total nitrogen and the lowest of protein nitrogen. The exogenous amino acid content in the embryo was higher than in cotyledons and testa. Both albumins and globulins were shown to contain 42% exogenous amino acids. The content of methionine - the first limiting amino acid of bean proteins - did not exceed 0.30% of the total amino acid content in albumins and globulins. Free glutamic and aspartic acids made up more than 60% of the total free amino acids.


1955 ◽  
Vol 8 (4) ◽  
pp. 537 ◽  
Author(s):  
DH Simmonds

The amino acid composition of 16-hr 6N HCI hydrolysates of three qualities of commercially classified wools has now been determined using the technique of Moore and Stein (1951). In this paper the results obtained on samples of Merino 70's and Corriedale 56's wool are compared with those previously reported for Merino wool of 64's quality. The overall pattern of the amino acid composition of the three wools is similar although small variations between the wools are observed with some of the amino acids.


1973 ◽  
Vol 134 (2) ◽  
pp. 431-436 ◽  
Author(s):  
W. Ferdinand ◽  
W. Bartley ◽  
V. Broomhead

Amino acid analyses of mitochondrial membranes are compared with the amino acid composition of whole mitochondria (Alberti, 1964) and found to be very similar except in the cystine content. The composition of the endogenous amino acids found in freshly prepared mitochondria has been established and shown to differ considerably from the amino acid composition of membranes or whole mitochondria. The amino acids produced during anaerobic incubation of mitochondria at pH7.4, on the other hand, resemble the membrane in composition, supporting the view that neutral proteinase activity is responsible for their appearance. Aerobic incubation produces a similar pattern of amino acids except that amino acids such as proline, serine, asparagine, glutamic acid and glutamine, which can be metabolically utilized under aerobic conditions, are present to a smaller extent. The presence of large relative concentrations of endogenous taurine, cysteic acid and oxidized glutathione and the accumulation of taurine during incubation is found. The selective retention of taurine and cysteic acid within the mitochondria is established. It is proposed that the first step in the degeneration of isolated mitochondria results from lipid hydroperoxide accumulation caused by the lack of glutathione reductase in isolated mitochondria.


1955 ◽  
Vol 102 (4) ◽  
pp. 435-440 ◽  
Author(s):  
Leonard T. Skeggs ◽  
Walton H. Marsh ◽  
Joseph R. Kahn ◽  
Norman P. Shumway

A preparation of hypertensin I was purified by countercurrent distribution and was shown to migrate as a single component in starch blocks at pH 9.3 and 4.2. It had an isoelectric point of 7.7. Quantitative analysis by ion exchange column chromatography showed eight amino acids in approximately unimolar proportion: aspartic, proline, valine, isoleucine, leucine, tyrosine, phenylalanine, and arginine. There were in addition two moles of histidine.


2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Karidia Konate ◽  
Emilie Josse ◽  
Milana Tasic ◽  
Karima Redjatti ◽  
Gudrun Aldrian ◽  
...  

AbstractRecently, we designed novel amphipathic cell-penetrating peptides, called WRAP, able to transfer efficiently siRNA molecules into cells. In order to gain more information about the relationship between amino acid composition, nanoparticle formation and cellular internalization of these peptides composed of only three amino acids (leucine, arginine and tryptophan), we performed a structure–activity relationship (SAR) study. First, we compared our WRAP1 and WRAP5 peptides with the C6M1 peptide also composed of the same three amino acids and showing similar behaviors in siRNA transfection. Afterwards, to further define the main determinants in the WRAP activity, we synthesized 13 new WRAP analogues harboring different modifications like the number and location of leucine and arginine residues, the relative location of tryptophan residues, as well as the role of the α-helix formation upon proline insertions within the native WRAP sequence. After having compared the ability of these peptides to form peptide-based nanoparticles (PBNs) using different biophysical methods and to induce a targeted gene silencing in cells, we established the main sequential requirements of the amino acid composition of the WRAP peptide. In addition, upon measuring the WRAP-based siRNA transfection ability into cells compared to several non-peptide transfection agents available on the markets, we confirmed that WRAP peptides induced an equivalent level of targeted gene silencing but in most of the cases with lower cell toxicity as clearly shown in clonogenic assays.


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