Separation of the tryptic peptides and cyanogen bromide fragments of the human embryonic zeta chains of hemoglobin in Portland I and II by reverse phase high performance liquid chromatography

The amino acid compositions of tryptic peptides and cyanogen bromide fragments of the purified zeta chain of Hb Portland I (zeta 2 gamma 2) and Hb Portland II (zeta 2 beta 2) have been determined. The hemoglobins were obtained from blood from neonates with hydrops fetalis due to homozygous alpha-tha...

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Bibliographic Details
Published in:	Hemoglobin Vol. 8; no. 5; p. 463
Main Authors:	Randhawat, Z I, Jones, R T, Lie-Injo, L E
Format:	Journal Article
Language:	English
Published:	England 1984
Subjects:	Amino Acid Sequence Amino Acids - analysis Chromatography, High Pressure Liquid Cyanogen Bromide Fetal Blood - analysis Globins - isolation & purification Hemoglobins, Abnormal - isolation & purification Humans Infant, Newborn Peptide Fragments - isolation & purification Thalassemia - blood Trypsin
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Summary:	The amino acid compositions of tryptic peptides and cyanogen bromide fragments of the purified zeta chain of Hb Portland I (zeta 2 gamma 2) and Hb Portland II (zeta 2 beta 2) have been determined. The hemoglobins were obtained from blood from neonates with hydrops fetalis due to homozygous alpha-thalassemia. The globin chains, tryptic peptides and cyanogen bromide fragments were all separated by reverse phase high performance liquid chromatography (HPLC). Several different types of C-18 columns were used with two different developer systems. The tryptic peptides of aminoethylated zeta chain were separated using an ammonium acetate-acetonitrile gradient. An aqueous trifuoroacetic acid-1-propanol developer gradient was used for the separation of cyanogen bromide fragments. Of the seventeen tryptic peptides obtained, two (zeta T10a and zeta T10b) resulted from the unusual cleavage of a Tyr-Ile peptide bond. This was observed even when using TPCK treated trypsin. From this study and results of others, it can be deduced that trypsin will hydrolyze the Tyr-X bond provided either Ala or Ile is bonded to the N-terminal side of Tyr and Ile, Leu, or Gly is bonded to the C-terminal side of the Tyr residue.
ISSN:	0363-0269
DOI:	10.3109/03630268408991732