2001
DOI: 10.1016/s0016-7037(00)00621-9
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Preservation of protein in marine systems: Hydrophobic and other noncovalent associations as major stabilizing forces

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Cited by 77 publications
(53 citation statements)
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“…In comparing our shipboard incubations to field collected material from the same location (Moore et al 2012a), it is striking that the number of identified proteins and ratios of THAA/OC and THAA-N/PN for incubations times of 22, 35, 47, and 53 d were very similar to those seen in deep basin sediments (3490 m), over wintered shelf sediments (101 m), and suspended particles (50 m, 100 m) of the Bering Sea. Although this finding suggests that the rapid protein losses seen in shipboard incubations are realistic, it also supports findings that intact proteins contribute to a fraction of marine sedimentary amino acids (Pantoja & Lee 1999, Nguyen & Harvey 2001, Nunn et al 2010, Moore et al 2012a. The distribution of remaining proteins observed after 22 d also indicates that abundant chloroplast proteins make up the majority of identified preserved proteins.…”
Section: Identifiable Protein Correlates To Organic Matter Degradatiosupporting
confidence: 80%
“…In comparing our shipboard incubations to field collected material from the same location (Moore et al 2012a), it is striking that the number of identified proteins and ratios of THAA/OC and THAA-N/PN for incubations times of 22, 35, 47, and 53 d were very similar to those seen in deep basin sediments (3490 m), over wintered shelf sediments (101 m), and suspended particles (50 m, 100 m) of the Bering Sea. Although this finding suggests that the rapid protein losses seen in shipboard incubations are realistic, it also supports findings that intact proteins contribute to a fraction of marine sedimentary amino acids (Pantoja & Lee 1999, Nguyen & Harvey 2001, Nunn et al 2010, Moore et al 2012a. The distribution of remaining proteins observed after 22 d also indicates that abundant chloroplast proteins make up the majority of identified preserved proteins.…”
Section: Identifiable Protein Correlates To Organic Matter Degradatiosupporting
confidence: 80%
“…These identified proteins represent material that may have been preserved after burial [12,[54][55][56][57] or mixed from the surface into deeper sediments by bioturbators [58][59][60]. Thus, it is expected that fewer proteins, with potentially lower sequence coverage, would be identified in the Bering Sea 8-to 10-cm core section than in surface sediments observed by Moore et al [16,29].…”
Section: Resultsmentioning
confidence: 89%
“…Peptides identified in smaller than expected molecular weight ranges could be due to partial hydrolysis [50]. Covalent modifications [13,51,52], hydrophobic interactions [12,13] and sequestration in potential energy fields [53] have been proposed as mechanisms for enhanced protein preservation, which could influence the gel migration of proteins to be in larger than expected molecular weight sections. The denaturing conditions of the SDS-PAGE gels used in this study indicate that charge alteration could also play a role in protein mobility.…”
Section: Resultsmentioning
confidence: 99%
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“…Two main mechanisms are accepted for OM transformation and preservation during diagenesis, catagenesis and metagenesis: degradation/recondensation (Tissot & Welte 1978) and selective preservation (Tegelaar et al 1989) (the discussion on the merits of each one is beyond the purpose of this work; see Largeau & Derenne 1993, Tyson 1995 for a discussion about this subject). Carbohydrates and proteins are regarded as components with low diagenetic preservation potential (although a fraction of these macromolecules can be preserved in sediments, see Nguyen & Harvey 2001, Jensen et al 2005 and references therein). Lipids, on the other hand, are thought to be more resistant.…”
Section: Biogeochemistry: High Lipid Content As Indicative Of Oxygen mentioning
confidence: 99%