2000
DOI: 10.1016/s0021-9673(99)01353-9
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Kinetics of appearance of hemorphins from bovine hemoglobin peptic hydrolysates by a direct coupling of reversed-phase high-performance liquid chromatography and electrospray ionization mass spectrometry

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Cited by 17 publications
(18 citation statements)
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“…These peptides contained an arginine basic residue in their sequence and had a hydrophobicity of about 1700 cal/mol, as the Bigelow scale [27], which was a high value compared with the average hydrophobicity of peptides produced during haemoglobin hydrolysis by pepsin which is about 1000 cal/mol. Moreover, these haemorphins were present in some very complex peptidic mixtures which contained more than hundreds of peptides with different sequence [29]. Fig.…”
Section: Recovery In the Absence Of Alkyl-sulfonic Acidsmentioning
confidence: 99%
“…These peptides contained an arginine basic residue in their sequence and had a hydrophobicity of about 1700 cal/mol, as the Bigelow scale [27], which was a high value compared with the average hydrophobicity of peptides produced during haemoglobin hydrolysis by pepsin which is about 1000 cal/mol. Moreover, these haemorphins were present in some very complex peptidic mixtures which contained more than hundreds of peptides with different sequence [29]. Fig.…”
Section: Recovery In the Absence Of Alkyl-sulfonic Acidsmentioning
confidence: 99%
“…16 In the present work the biotransformation process from the antimicrobial peptide α107-136 to the bradykinin-potentiating peptide α110-125 was extensively investigated during peptic hydrolysis of bovine haemoglobin. Compared with the precursor haemorphin LVVH-7 (β31-40) studied previously, 7,8 the antibacterial peptide α107-136 has many more cleavage sites for pepsin in the sequence. It is for this reason that the diversity of the reaction components in our experiment is much greater than that in earlier studies.…”
Section: Introductionmentioning
confidence: 94%
“…Such was the case with the biotransformation of one haemorphin to another in previous studies. 7,8 These haemorphins were all found in the 31-40 region of the bovine haemoglobin β-chain. Their release kinetics was typically followed by liquid chromatography coupled with either photodiode array detection 7 or mass spectrometry.…”
Section: Introductionmentioning
confidence: 99%
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“…Experimental procedure of peptidic hydrolysates coupled RP-HPLC-MS was performed according to the literature [10].…”
Section: Coupling Of Rp-hplc and Esi-msmentioning
confidence: 99%