Molecular cloning and sequence analysis of bovine lactotransferrin

FEBS Journal - Tập 196 Số 1 - Trang 177-184 - 1991
Annick Pierce1, Didier Colavizza, Monique Benaı̈ssa, P Maes, Aurélien Tartar, J Montreuil, G Spik
1Laboratoire de Chimie Biologique (Unité Mixte de Recherche no. 111 du Centre National de la Recherche Scientifique), Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France.

Tóm tắt

The screening of a bovine submaxillary gland cDNA library yielded 25 clones coding for bovine lactotransferrin. The nucleotide sequence of the longest insert contained a protein‐coding region of 2115 nucleotides and a 3′ non‐coding region of 194 nucleotides followed by a poly(A) tract of about 55 nucleotides. The predicted peptide sequence included a 16‐amino‐acid signal sequence upstream of the first amino acid of the native protein. The identity of the clone was confirmed by matching the amino acid sequence predicted from the cDNA with the N‐terminal and tryptic peptide sequences derived from purified bovine milk lactotransferrin, and also by similarity with human and murine lactotransferrins. The cDNA described corresponds to a 705‐amino‐acid‐long preprotein that lacks the start methionine. The sequence of the secreted protein is 689 amino acids long and contains five potential glycosylation sites. Bovine lactotransferrin is 69% and 64% identical to human and murine lactotransferrins, respectively.

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Tài liệu tham khảo

10.1146/annurev.bi.49.070180.002041

Montreuil J., 1985, Proteins of iron storage and transport, 25

Montreuil J., 1960, C. R. Acad. Sci. Paris, 250, 1736

10.1016/0006-3002(60)91478-5

10.3891/acta.chem.scand.14-0510

10.1021/ja01498a029

10.1126/science.152.3729.1626

Masson P. L., 1970, La lactoferrine, protéine des sécrétions externes et des leucocytes neutrophiles

Biserte G., 1963, Exp. Ann. Biochem. Med., 25, 85

10.1084/jem.130.3.643

10.1182/blood.V64.5.1103.1103

Spik G., 1983, Bull. Physiopathol. Resp., 19, 123

Spik G., 1985, Proteins of iron storage and transport

Fletcher J., 1989, Iron in immunity, cancer and inflammation, 223

10.1111/j.1432-1033.1984.tb08607.x

Rado T. A., 1987, Blood, 70, 989, 10.1182/blood.V70.4.989.989

10.1016/0022-2836(89)90602-5

10.1111/j.1432-1033.1982.tb05803.x

10.1016/S0021-9258(18)61088-9

10.1042/bj2470571

Wang C. S., 1984, Comp. Biochem. Physiol., 78, 575, 10.1016/0300-9629(84)90599-1

Halbeek H., 1981, Biochim. Biophys. Acta, 685, 293

10.1016/0300-9084(88)90283-0

10.1016/0005-2795(76)90112-4

10.1007/978-1-349-06375-8_5

Legrand D., 1990, Biochem. J., 266, 575

10.1016/0022-2836(86)90432-8

Sambroock J., 1989, Molecular cloning

10.1073/pnas.69.6.1408

10.1016/S0003-2697(76)80049-8

10.1016/0006-291X(84)91648-6

10.1016/0378-1119(83)90230-5

10.1093/nar/7.6.1513

10.1073/pnas.74.12.5463

10.1093/nar/9.12.2871

Chéron A., 1977, C. R. Acad. Sci. Paris, 284, 585

10.1016/S0076-6879(67)11022-7

10.1016/0167-4838(84)90111-0

10.1007/BF01534490

10.1007/BF01958861

10.1016/0968-0004(82)90183-9

10.1016/0300-9084(88)90184-8

10.1016/0968-0004(87)90163-0

10.1016/S0065-2318(08)60433-3

10.1016/0167-4838(89)90015-0

10.1016/0014-5793(84)80937-0

10.1203/00006450-198602000-00021

Gillivray R. T. A., 1983, J. Biol. Chem., 258, 3543, 10.1016/S0021-9258(18)32696-6

10.1073/pnas.81.9.2752

10.1016/0006-291X(84)91185-9

10.1111/j.1432-1033.1982.tb05879.x

10.1111/j.1432-1033.1982.tb05880.x

10.1073/pnas.83.5.1261

10.1111/j.1432-1033.1983.tb07424.x

10.1021/bi00429a001

10.1016/0022-2836(85)90046-4