Bovine alpha 1-microglobulin/bikunin. Isolation and characterization of liver cDNA and urinary alpha 1-microglobulin
(1996) In Biochimica et Biophysica Acta 1306(1). p.98-106- Abstract
cDNA coding for alpha 1-microglobulin, an immunoregulatory plasmaprotein, was isolated from bovine liver. The sequence of a total of 1258 nucleotides revealed an open reading frame of 352 amino acids. This included alpha 1-microglobulin, 182 amino acids, and bikunin, the light chain of the plasmaprotein inter-alpha-inhibitor, 147 amino acids. The two proteins were connected by a basic tetrapeptide, R-A-R-R, which conforms to the consensus sequence recognized by endoproteolytic cleavage enzymes. The deduced amino acid sequence showed a high degree of identity with alpha 1-microglobulin and bikunin sequences from other species, and the alpha 1-microglobulin part displayed sequence motifs typical for members of the lipocalin protein... (More)
cDNA coding for alpha 1-microglobulin, an immunoregulatory plasmaprotein, was isolated from bovine liver. The sequence of a total of 1258 nucleotides revealed an open reading frame of 352 amino acids. This included alpha 1-microglobulin, 182 amino acids, and bikunin, the light chain of the plasmaprotein inter-alpha-inhibitor, 147 amino acids. The two proteins were connected by a basic tetrapeptide, R-A-R-R, which conforms to the consensus sequence recognized by endoproteolytic cleavage enzymes. The deduced amino acid sequence showed a high degree of identity with alpha 1-microglobulin and bikunin sequences from other species, and the alpha 1-microglobulin part displayed sequence motifs typical for members of the lipocalin protein superfamily. A single alpha 1-microglobulin/bikunin mRNA with a size of around 1300 nt was found in bovine liver. The mature alpha 1-microglobulin protein was isolated from bovine urine, and partly characterized. It was found to be a globular molecule with an apparent molecular weight of 23,300, containing one N-linked and at least on O-linked oligosaccharide, one intra-chain disulfide bridge and an electrophoretic heterogeniety with a pI-value of 4.1-5.2.
(Less)
- author
- Lindqvist, A LU and Akerström, B LU
- organization
- publishing date
- 1996-04-10
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Alpha-Globulins/genetics, Amino Acid Sequence, Animals, Base Sequence, Cattle/genetics, Cricetinae, DNA, Complementary/genetics, Female, Genes, Gerbillinae, Glycoproteins/genetics, Glycosylation, Guinea Pigs, Humans, Liver/metabolism, Membrane Glycoproteins, Molecular Sequence Data, Molecular Weight, Open Reading Frames, Pregnancy, Protein Processing, Post-Translational, Rabbits, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity, Trypsin Inhibitor, Kunitz Soybean, Urine/chemistry
- in
- Biochimica et Biophysica Acta
- volume
- 1306
- issue
- 1
- pages
- 98 - 106
- publisher
- Elsevier
- external identifiers
-
- pmid:8611630
- scopus:0029925597
- ISSN
- 0006-3002
- DOI
- 10.1016/0167-4781(95)00235-9
- language
- English
- LU publication?
- yes
- id
- c8635079-89db-415c-832e-7960a7381a06
- date added to LUP
- 2019-05-22 10:19:01
- date last changed
- 2024-01-01 06:41:13
@article{c8635079-89db-415c-832e-7960a7381a06,
abstract = {{<p>cDNA coding for alpha 1-microglobulin, an immunoregulatory plasmaprotein, was isolated from bovine liver. The sequence of a total of 1258 nucleotides revealed an open reading frame of 352 amino acids. This included alpha 1-microglobulin, 182 amino acids, and bikunin, the light chain of the plasmaprotein inter-alpha-inhibitor, 147 amino acids. The two proteins were connected by a basic tetrapeptide, R-A-R-R, which conforms to the consensus sequence recognized by endoproteolytic cleavage enzymes. The deduced amino acid sequence showed a high degree of identity with alpha 1-microglobulin and bikunin sequences from other species, and the alpha 1-microglobulin part displayed sequence motifs typical for members of the lipocalin protein superfamily. A single alpha 1-microglobulin/bikunin mRNA with a size of around 1300 nt was found in bovine liver. The mature alpha 1-microglobulin protein was isolated from bovine urine, and partly characterized. It was found to be a globular molecule with an apparent molecular weight of 23,300, containing one N-linked and at least on O-linked oligosaccharide, one intra-chain disulfide bridge and an electrophoretic heterogeniety with a pI-value of 4.1-5.2.</p>}},
author = {{Lindqvist, A and Akerström, B}},
issn = {{0006-3002}},
keywords = {{Alpha-Globulins/genetics; Amino Acid Sequence; Animals; Base Sequence; Cattle/genetics; Cricetinae; DNA, Complementary/genetics; Female; Genes; Gerbillinae; Glycoproteins/genetics; Glycosylation; Guinea Pigs; Humans; Liver/metabolism; Membrane Glycoproteins; Molecular Sequence Data; Molecular Weight; Open Reading Frames; Pregnancy; Protein Processing, Post-Translational; Rabbits; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Trypsin Inhibitor, Kunitz Soybean; Urine/chemistry}},
language = {{eng}},
month = {{04}},
number = {{1}},
pages = {{98--106}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Bovine alpha 1-microglobulin/bikunin. Isolation and characterization of liver cDNA and urinary alpha 1-microglobulin}},
url = {{http://dx.doi.org/10.1016/0167-4781(95)00235-9}},
doi = {{10.1016/0167-4781(95)00235-9}},
volume = {{1306}},
year = {{1996}},
}