scholarly journals Abnormal (hydroxy)prolines deuterium content redefines hydrogen chemical mass

2021 ◽  
Author(s):  
Hassan Gharibi ◽  
Alexey L Chernobrovkin ◽  
Gunilla Eriksson ◽  
Amirata Saei Dibavar ◽  
Zena Timmons ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bone Collagen ◽  
Deuterium Content ◽  
Plausible Mechanism

Analyzing the δ2H in individual amino acids of proteins extracted from vertebrates, we unexpectedly found in some samples, notably bone collagen from seals, more than twice as much deuterium in proline and hydroxyproline residues than in seawater. This corresponds to at least four times higher δ2H than in any previously reported biogenic sample. We ruled out diet as a plausible mechanism for such anomalous enrichment. This finding puts into question the old adage that you are what you eat.

scholarly journals COLLAGEN METABOLISM IN THE NORMAL AND LATHYRITIC CHICK

1964 ◽  
Vol 119 (2) ◽  
pp. 275-289 ◽  
Author(s):  
Marvin L. Tanzer ◽  
Jerome Gross
Keyword(s):  
Amino Acids ◽  
Chick Embryo ◽  
Collagen Synthesis ◽  
Fibril Formation ◽  
Collagen Metabolism ◽  
Bone Collagen ◽  
Double Labeling

1. Radioisotope incorporation studies of normal and lathyritic chick embryo bone collagen do not demonstrate any interference by lathyrism with collagen synthesis or fibril formation. 2. The results indicate that a portion of the extractable collagen from lathyritic chick embryo bone represents newly synthesized protein. Evidence from a double labeling experiment and from analysis of isotope flow between the extractable and non-extractable pools suggests the extractable lathyritic collagen is heterogeneous. We propose that the lathyritic process affects collagen in all states of aggregation, probably in varying degree. 3. Puromycin, administered intravenously, reduces the amount of extractable collagen in both normal and lathyritic chick embryo bone, and diminishes the incorporation of labeled proline into collagen. 4. Marked fluctuations in incorporation of labeled amino acids into chick embryo bone collagen suggests the occurrence of wide fluctuations in metabolism of this protein.

Analysis of Bone “Collagen” Extraction Products for Radiocarbon Dating

Radiocarbon ◽  
2013 ◽  
Vol 55 (2) ◽  
pp. 445-463 ◽  
Author(s):  
F Brock ◽  
V Geoghegan ◽  
B Thomas ◽  
K Jurkschat ◽  
T F G Higham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Radiocarbon Dating ◽  
Fulvic Acids ◽  
Bone Collagen ◽  
Low Molecular Weight ◽  
Extraction Procedures ◽  
Molecular Weights ◽  
Published Evidence ◽  
Inorganic Species

Archaeological bones are now routinely dated in many radiocarbon laboratories through the extraction of “collagen.” Methods for “collagen” extraction vary, and several laboratories now apply an ultrafiltration step after gelatinization to extract the higher molecular weight (usually >10 or 30kDa) fraction for dating, thereby removing low molecular weight contaminants. Ultrafiltration has been demonstrated to result in products that are easier to handle and have more acceptable C:N ratios, and in some instances can result in significantly improved (generally older) 14C dates when compared to non-ultrafiltered products from the same bone. Although it has been suggested that ultrafiltration removes potential contaminants such as short-chain degraded collagen and other peptides and amino acids, fulvic acids, and salts, there remains little published evidence to support this. This paper presents data from a pilot study investigating the most suitable techniques with which to study the products of the routine “collagen” extraction procedures employed at the Oxford Radiocarbon Accelerator Unit (ORAU) (modified Longin followed by ultrafiltration). The preliminary data demonstrates that the final product of “collagen” extraction at ORAU appears to be an aggregate consisting of a range of proteins of different molecular weights, including collagen, as well as some other organic matter and inorganic species. Ultrafiltration is removing some, but not all, of the <30kDa fraction from the samples. Further work to investigate the nature of this aggregate and how best to improve the efficiency of “collagen” extraction procedures is discussed.

scholarly journals Quantifying dietary macronutrient sources of carbon for bone collagen biosynthesis using natural abundance stable carbon isotope analysis

2006 ◽  
Vol 95 (6) ◽  
pp. 1055-1062 ◽  
Author(s):  
Susan Jim ◽  
Vicky Jones ◽  
Stanley H. Ambrose ◽  
Richard P. Evershed
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
De Novo ◽  
Stable Carbon Isotope ◽  
Isotopic Fractionation ◽  
Essential Amino Acids ◽  
Natural Abundance ◽  
Bone Collagen ◽  
Collagen Biosynthesis ◽  
Indispensable Amino Acids

The diets of laboratory rats were isotopically and nutritionally manipulated using purifiedC3 and/or C4 macronutrients to investigate the routing of dietary carbonto bone collagen biosynthesis. Diets were formulated with purified proteins, carbohydrates andlipids of defined composition and natural abundance stable isotope ratios. Bulk protein and constituent amino acid δ13C values determined for whole diet and bone collagen provided the basis for assessing isotopic fractionation and estimating the degree of routing versus synthesis de novo of essential, non-essential and conditionally indispensable amino acids. Essential and conditionally indispensable amino acids were shown to be routed from diet to collagen with little isotopic fractionation whereas non-essential amino acids differed by up to 20‰. Mathematical modelling of the relationships between macronutrient and tissue δ13C values provided qualitative and quantitative insights into the metabolic and energetic controls on bone collagen biosynthesis. Essential amino acids comprise 21·7% of the carbon in collagen, defining the minimum amount of dietary carbon routing. Estimates of 42 and 28% routing were shown for the non-essential amino acids, glycine and aspartate, respectively. In total, the routing of non-essential and conditionally indispensable amino acids was estimated to equal 29·6% of the carbon in collagen. When the contribution of carbon from the essential amino acids is also considered, we arrive at an overall minimum estimate of 51·3% routing of dietary amino acid carbon into bone collagen.

scholarly journals Dynamics of Polymer Membrane Swelling in Aqueous Suspension of Amino-Acids with Different Isotopic Composition; Photoluminescence Spectroscopy Experiments

Polymers ◽  
2021 ◽  
Vol 13 (16) ◽  
pp. 2635
Author(s):  
Nikolai F. Bunkin ◽  
Polina N. Bolotskova ◽  
Elena V. Bondarchuk ◽  
Valery G. Gryaznov ◽  
Valeriy A. Kozlov ◽  
...  
Keyword(s):  
Amino Acids ◽  
Aqueous Suspension ◽  
Membrane Surface ◽  
Polymer Membrane ◽  
Photoluminescence Spectroscopy ◽  
Polymer Fibers ◽  
Deuterium Content ◽  
Ordinary Water ◽  
Liquid Bulk ◽  
Deuterium Depleted Water

In photoluminescence spectroscopy experiments, the interaction mode of the polymer membrane Nafion with various amino-acids was studied. The experiments were performed with physiological NaCl solutions prepared in an ordinary water (the deuterium content is 157 ± 1 ppm) and also in deuterium-depleted water (the deuterium content is ≤1 ppm). These studies were motivated by the fact that when Nafion swells in ordinary water, the polymer fibers are effectively “unwound” into the liquid bulk, while in the case of deuterium-depleted water, the unwinding effect is missing. In addition, polymer fibers, unwound into the liquid bulk, are similar to the extracellular matrix (glycocalyx) on the cell membrane surface. It is of interest to clarify the role of unwound fibers in the interaction of amino-acids with the polymer membrane surface. It turned out that the interaction of amino-acids with the membrane surface gives rise to the effects of quenching luminescence from the luminescence centers. We first observed various dynamic regimes arising upon swelling the Nafion membrane in amino-acid suspension with various isotopic content, including triggering effects, which is similar to the processes in the logical gates of computers.

scholarly journals Radiocarbon Dating of Individual Amino Acids from Archaeological Bone Collagen

Radiocarbon ◽  
2010 ◽  
Vol 52 (2) ◽  
pp. 620-634 ◽  
Author(s):  
James S O McCullagh ◽  
Anat Marom ◽  
Robert E M Hedges
Keyword(s):  
Amino Acids ◽  
Radiocarbon Dating ◽  
Sample Pretreatment ◽  
Bone Collagen ◽  
Small Samples ◽  
Successful Isolation ◽  
Soil Components ◽  
The 1960S ◽  
The Individual ◽  
Quaternary Paleoecology

Since the development of accelerator mass spectrometry (AMS) for radiocarbon dating in the late 1970s, its ability to date small samples of bone has been of huge importance in archaeology and Quaternary paleoecology. The conventional approach to sample preparation has been to extract and gelatinize protein, which is then combusted and graphitized for analysis. However, this “bulk protein” can contain a heterogeneous mixture of non-collagenous molecules, including humic acids and other soil components that may be of a different age than the bone and therefore affect the accuracy of its 14C date. Sample pretreatment methods have been an important area of development in recent years but still show inadequacies for the dating of severely contaminated bone. The idea of isolating and dating individual compounds such as single amino acids, to improve dating accuracy, has been discussed in the literature since the 1960s. Hydroxyproline, for example, makes up over 10% of bone collagen but is extremely rare in most other animal proteins, increasing the chances of its presence being endogenous to the individual being dated. Its successful isolation has therefore been considered a potential “gold standard” for dating archaeological bone; however, extracting and suitably purifying single amino acids from bone has proved a challenging task.

scholarly journals Dietary Reconstruction of the Okhotsk Culture of Hokkaido, Japan, Based on Nitrogen Composition of Amino Acids: Implications for Correction of 14C Marine Reservoir Effects on Human Bones

Radiocarbon ◽  
2010 ◽  
Vol 52 (2) ◽  
pp. 671-681 ◽  
Author(s):  
Yuichi I Naito ◽  
Yoshito Chikaraishi ◽  
Naohiko Ohkouchi ◽  
Hitoshi Mukai ◽  
Yasuyuki Shibata ◽  
...  
Keyword(s):  
Amino Acids ◽  
Isotopic Composition ◽  
Glutamic Acid ◽  
Bone Collagen ◽  
Human Populations ◽  
Radiocarbon Age ◽  
Carbon And Nitrogen ◽  
Relative Contribution ◽  
Fur Seal ◽  
Nitrogen Isotopic Composition

The relative contribution of marine-derived carbon in the ancient diet is essential for correcting the marine reservoir effect on the radiocarbon age of archaeological human remains. In this study, we evaluated the marine protein consumption of 3 human populations from the Okhotsk culture (about AD 550–1200) in Hokkaido, Japan, based on stable carbon and nitrogen isotopic compositions in bulk bone collagen as well as the nitrogen isotopic composition of glutamic acid and phenylalanine. Despite the similarity of carbon and nitrogen isotopic composition of bulk collagens, nitrogen isotopic composition of their constituent amino acids suggests differences in fur seal contributions among northern Hokkaido (0–24% for Kafukai 1, 0–10% for Hamanaka 2) and eastern Hokkaido (78–80% for Moyoro) populations. It suggests that nitrogen composition of glutamic acid and phenylalanine could provide a detailed picture of ancient human subsistence.

scholarly journals Routine AMS Dating of Bone and Shell Proteins

Radiocarbon ◽  
1986 ◽  
Vol 28 (2A) ◽  
pp. 451-456 ◽  
Author(s):  
Richard Gillespie ◽  
R E M Hedges ◽  
M J Humm
Keyword(s):  
Amino Acids ◽  
Insoluble Fraction ◽  
Bone Collagen ◽  
Dilute Acid ◽  
Isolation And Purification ◽  
Insoluble Collagen ◽  
Shell Proteins ◽  
Burned Bone ◽  
Ams Dating ◽  
Single Method

14C dating of bone has been unreliable in comparison with more stable materials such as wood or charcoal. Attempts have been made to use various components or fractions isolated from the raw bone sample; these include dilute acid soluble, dilute acid insoluble, collagen, and gelatin, as well as alkali soluble and insoluble fractions of burned bone, and carbonate or apatite fractions of organic-poor bone. All of these fractions have yielded useful data in some cases, but no single method has proven suitable in all situations. The work reported here describes the isolation and purification of amino acids from the dilute acid insoluble fraction of bone collagen and parchment, with some preliminary experiments on amino acids from shell conchiolin.

scholarly journals Exceptionally high δ15N values in collagen single amino acids confirm Neandertals as high-trophic level carnivores

2019 ◽  
Vol 116 (11) ◽  
pp. 4928-4933 ◽  
Author(s):  
Klervia Jaouen ◽  
Michael P. Richards ◽  
Adeline Le Cabec ◽  
Frido Welker ◽  
William Rendu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Freshwater Fish ◽  
Transition Period ◽  
Isotope Ratios ◽  
Trophic Levels ◽  
Upper Paleolithic ◽  
Bone Collagen ◽  
Single Amino Acid ◽  
Large Herbivores ◽  
C And N

Isotope and archeological analyses of Paleolithic food webs have suggested that Neandertal subsistence relied mainly on the consumption of large herbivores. This conclusion was primarily based on elevated nitrogen isotope ratios in Neandertal bone collagen and has been significantly debated. This discussion relies on the observation that similar high nitrogen isotopes values could also be the result of the consumption of mammoths, young animals, putrid meat, cooked food, freshwater fish, carnivores, or mushrooms. Recently, compound-specific C and N isotope analyses of bone collagen amino acids have been demonstrated to add significantly more information about trophic levels and aquatic food consumption. We undertook single amino acid C and N isotope analysis on two Neandertals, which were characterized by exceptionally high N isotope ratios in their bulk bone or tooth collagen. We report here both C and N isotope ratios on single amino acids of collagen samples for these two Neandertals and associated fauna. The samples come from two sites dating to the Middle to Upper Paleolithic transition period (Les Cottés and Grotte du Renne, France). Our results reinforce the interpretation of Neandertal dietary adaptations as successful top-level carnivores, even after the arrival of modern humans in Europe. They also demonstrate that high δ15N values of bone collagen can solely be explained by mammal meat consumption, as supported by archeological and zooarcheological evidence, without necessarily invoking explanations including the processing of food (cooking, fermenting), the consumption of mammoths or young mammals, or additional (freshwater fish, mushrooms) dietary protein sources.

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