PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3101598-2 1987 In order to identify the residues that were phosphorylated, the A alpha-chain of fibrinogen was isolated and subjected to consecutive cleavage by cyanogen bromide, trypsin, and chymotrypsin. Cyanogen Bromide 146-162 fibrinogen beta chain Homo sapiens 81-91 3122725-0 1987 The interaction of streptokinase.plasminogen activator complex, tissue-type plasminogen activator, urokinase and their acylated derivatives with fibrin and cyanogen bromide digest of fibrinogen. Cyanogen Bromide 156-172 fibrinogen beta chain Homo sapiens 183-193 3563970-8 1986 The same peptide was also isolated following cyanogen bromide treatment of the intact fibrinogen Perugia. Cyanogen Bromide 45-61 fibrinogen beta chain Homo sapiens 86-96 4040660-0 1985 Species specificity in the acceleration of tissue-type plasminogen activator-mediated activation of plasminogens, by fibrinogen cyanogen bromide fragments. Cyanogen Bromide 128-144 fibrinogen beta chain Homo sapiens 117-127 3930491-11 1985 The binding of TSP to fibrinogen-Sepharose was quantitatively blocked by pretreatment with an antibody to the cyanogen bromide cleavage fragment composed of residues 241-476 of the carboxyl-terminal end of the alpha chain of fibrinogen. Cyanogen Bromide 110-126 fibrinogen beta chain Homo sapiens 22-32 3930491-11 1985 The binding of TSP to fibrinogen-Sepharose was quantitatively blocked by pretreatment with an antibody to the cyanogen bromide cleavage fragment composed of residues 241-476 of the carboxyl-terminal end of the alpha chain of fibrinogen. Cyanogen Bromide 110-126 fibrinogen beta chain Homo sapiens 225-235 3708159-7 1986 An abnormal peptide was isolated after cyanogen bromide cleavage of intact fibrinogen Milano l. This fragment spans from position gamma 311 to gamma 336. Cyanogen Bromide 39-55 fibrinogen beta chain Homo sapiens 75-85 139916-8 1977 The overlap with key cyanogen bromide fragments has also allowed us to propose an order for the first 198 residues of the fibrinogen alpha chain. Cyanogen Bromide 21-37 fibrinogen beta chain Homo sapiens 122-132 6719396-3 1984 By consecutive cleavage of the A alpha-chains of fetal and adult fibrinogen with cyanogen bromide, trypsin, and chymotrypsin, separation of the resulting peptide mixtures and analysis for phosphorylated amino acids, this second phosphorylation site could be traced to Ser 345 of the A alpha-chain. Cyanogen Bromide 81-97 fibrinogen beta chain Homo sapiens 65-75 6681716-2 1983 However, when fibrin and fibrinogen are digested with cyanogen bromide, both digests potentiate the t-PA-mediated plasminogen activation equally well. Cyanogen Bromide 54-70 fibrinogen beta chain Homo sapiens 25-35 6941244-6 1981 Fragments from antibodies raised against a cyanogen bromide fragment of fibrinogen alpha chains (residues 241-476) also led to exclusive derivatization of the terminal domains, although in these cases the additional material was often separated discretely from the terminal sphere by a gap. Cyanogen Bromide 43-59 fibrinogen beta chain Homo sapiens 72-82 518844-2 1979 The largest fragment produced by complete cyanogen bromide digestion of the alpha chain of human fibrinogen contains 236 residues and has a calculated molecular weight of 23,949. Cyanogen Bromide 42-58 fibrinogen beta chain Homo sapiens 97-107 158526-2 1979 The cyanogen bromide fragment, N-DSK, containing the NH2-terminal portions of the three chains of fibrinogen, was found to exist in dimeric and polymeric forms. Cyanogen Bromide 4-20 fibrinogen beta chain Homo sapiens 98-108 420779-5 1979 The arrangement of the cyanogen bromide peptides was deduced by the use of overlap fragments obtained from the tryptic digestion of modified and unmodified beta-chains and from digestions with staphylococcal protease, as well as by considerations involving the plasmic digestion products of fibrinogen. Cyanogen Bromide 23-39 fibrinogen beta chain Homo sapiens 291-301 273904-4 1978 Most of the other cyanogen bromide fragments can be aligned by homology with the alpha and/or gamma chains from human fibrinogen, although the positioning of a few of the smallest peptides is still ambiguous. Cyanogen Bromide 18-34 fibrinogen beta chain Homo sapiens 118-128 738701-3 1978 When fibrinogen is cleaved by cyanogen bromide five disulfide-containing fragments are formed. Cyanogen Bromide 30-46 fibrinogen beta chain Homo sapiens 5-15 851527-2 1977 Fully cross-linked human fibrin was digested with cyanogen bromide and the resulting fragments were characterized and compared with the fragments produced upon cyanogen bromide treatment of fibrinogen alpha chains. Cyanogen Bromide 160-176 fibrinogen beta chain Homo sapiens 190-200 851527-5 1977 The identified sequences corresponded to two cyanogen bromide fragments previously found in alpha chains isolated from fibrinogen, one of which has a molecular weight of about 30 000 and the other 6000. Cyanogen Bromide 45-61 fibrinogen beta chain Homo sapiens 119-129 4202821-0 1973 Identification of a large fragment after limited cyanogen bromide cleavage of fibrinogen. Cyanogen Bromide 49-65 fibrinogen beta chain Homo sapiens 78-88 124585-0 1975 Amino acid sequence of the carboxy-terminal cyanogen bromide peptide of the human fibrinogen beta-chain: homology with the corresponding gamma-chain peptide and presence in fragment D. The carboxy-terminal cyanogen bromide fragment of the human fibrinogen beta-chain has been isolated and its structure determined. Cyanogen Bromide 44-60 fibrinogen beta chain Homo sapiens 82-103 124585-0 1975 Amino acid sequence of the carboxy-terminal cyanogen bromide peptide of the human fibrinogen beta-chain: homology with the corresponding gamma-chain peptide and presence in fragment D. The carboxy-terminal cyanogen bromide fragment of the human fibrinogen beta-chain has been isolated and its structure determined. Cyanogen Bromide 206-222 fibrinogen beta chain Homo sapiens 82-103 124585-0 1975 Amino acid sequence of the carboxy-terminal cyanogen bromide peptide of the human fibrinogen beta-chain: homology with the corresponding gamma-chain peptide and presence in fragment D. The carboxy-terminal cyanogen bromide fragment of the human fibrinogen beta-chain has been isolated and its structure determined. Cyanogen Bromide 206-222 fibrinogen beta chain Homo sapiens 245-266 5012319-1 1972 I. Clevage of fibrinogen with cyanogen bromide. Cyanogen Bromide 30-46 fibrinogen beta chain Homo sapiens 14-24 11946783-0 1972 Amino acid sequence of the carboxy-terminal cyanogen bromide fragment from bovine and human fibrinogen gamma-chains. Cyanogen Bromide 44-60 fibrinogen beta chain Homo sapiens 92-102 4266974-0 1973 Characterisation of large fragments rich in disulphide bridges from CNBr-treated products of exhaustive proteolysis of fibrinogen by plasmin. Cyanogen Bromide 68-72 fibrinogen beta chain Homo sapiens 119-129 24319981-4 2013 According to our modification, the cyanogen bromide fragments of human fibrinogen have been changed into bovine desAB-fibrin. Cyanogen Bromide 35-51 fibrinogen beta chain Homo sapiens 71-81 1839461-3 1991 Activation of diabetic Pg by normal t-PA in the presence of stimulating CNBr fragments of fibrinogen exhibited a prolonged lag phase (30 to 60 minutes) until maximally stimulated plasmin formation occurred (normal, 5 to 15 minutes) and substrate inhibition at Pg concentrations more than 10 to 30 nM. Cyanogen Bromide 72-76 fibrinogen beta chain Homo sapiens 90-100 18180617-5 2008 In the present study, the effect of lysine or cyanogen bromide-treated fibrinogen, alone or in combination with the oversulfated compounds, on the activation of glutamic plasminogen by tissue plasminogen activator was investigated. Cyanogen Bromide 46-62 fibrinogen beta chain Homo sapiens 71-81 18180617-7 2008 Cyanogen bromide-treated fibrinogen (50 microg/ml) gave a 10-fold enhancement of activation by itself, and addition of 2.86 microg/ml oversulfated compounds amplified this to 15-fold. Cyanogen Bromide 0-16 fibrinogen beta chain Homo sapiens 25-35 2334691-2 1990 This peptide was isolated from cyanogen bromide degraded human fibrinogen and was investigated by 1H NMR (500 MHz) spectroscopy. Cyanogen Bromide 31-47 fibrinogen beta chain Homo sapiens 63-73 2617471-4 1989 We now report the detection of an abnormal peptide in a comparative peptide map from a cyanogen bromide digest of fibrinogen Baltimore IV. Cyanogen Bromide 87-103 fibrinogen beta chain Homo sapiens 114-124