1984
DOI: 10.1016/0049-3848(84)90359-1
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Quantitation of the three normally occurring plasma fibrinogens in health and during socalled “acute phase” by SDS electro-phoresis of fibrin obtained from EDTA-plasma

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Cited by 56 publications
(42 citation statements)
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“…Typical plasma-derived fibrinogen contains a major fraction with intact ␣C regions, HMW-Fg (50 -70%), and a minor fraction with one or two ␣C regions degraded, LMW-Fg and LMWЈ-Fg, respectively (44,45). The fraction with both ␣C regions truncated is elevated in patients with peripheral vascular diseases, liver disease, or diabetes and in the elderly (27)(28)(29)45). A substantial amount of the molecules without the ␣C regions is produced during thrombolytic therapy (46).…”
Section: Discussionmentioning
confidence: 99%
“…Typical plasma-derived fibrinogen contains a major fraction with intact ␣C regions, HMW-Fg (50 -70%), and a minor fraction with one or two ␣C regions degraded, LMW-Fg and LMWЈ-Fg, respectively (44,45). The fraction with both ␣C regions truncated is elevated in patients with peripheral vascular diseases, liver disease, or diabetes and in the elderly (27)(28)(29)45). A substantial amount of the molecules without the ␣C regions is produced during thrombolytic therapy (46).…”
Section: Discussionmentioning
confidence: 99%
“…The observed peaks primarily show the tyrosine/phenylalanine twisting doublet at 621/642 cm 1 while the 35 tyrosine ring breathing doublet can be seen at 829/860 cm 1 . The sharpest and most dominant peak at 1003 cm 1 is attributed to the phenylalanine symmetric breathing mode while CH 2 bending appears at 1446 cm 1 and the C=O stretching mode of Amide I at 1657 cm 1 . The Raman spectrum of crystalline fibrinogen 40 contains similar features, but notably has strong contributions from tryptophan at 758 cm 1 and 1552 cm 1 .…”
Section: Resultsmentioning
confidence: 99%
“…The sharpest and most dominant peak at 1003 cm 1 is attributed to the phenylalanine symmetric breathing mode while CH 2 bending appears at 1446 cm 1 and the C=O stretching mode of Amide I at 1657 cm 1 . The Raman spectrum of crystalline fibrinogen 40 contains similar features, but notably has strong contributions from tryptophan at 758 cm 1 and 1552 cm 1 . This is surprising as fibrinogen does not have a high tryptophan content, but may be due to sample impurities or alignment of tryptophan moieties in the crystalline sample.…”
Section: Resultsmentioning
confidence: 99%
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