Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4869
pubmed:dateCreated
1988-9-23
pubmed:databankReference
pubmed:abstractText
Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
241
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1098-101
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2842863-Amino Acid Sequence, pubmed-meshheading:2842863-Animals, pubmed-meshheading:2842863-Base Sequence, pubmed-meshheading:2842863-Carcinoma, Hepatocellular, pubmed-meshheading:2842863-Chromosome Mapping, pubmed-meshheading:2842863-Chromosomes, Human, Pair 10, pubmed-meshheading:2842863-DNA, pubmed-meshheading:2842863-Glycoproteins, pubmed-meshheading:2842863-Humans, pubmed-meshheading:2842863-Liver Neoplasms, pubmed-meshheading:2842863-Male, pubmed-meshheading:2842863-Mice, pubmed-meshheading:2842863-Mice, Nude, pubmed-meshheading:2842863-Molecular Sequence Data, pubmed-meshheading:2842863-Nucleic Acid Hybridization, pubmed-meshheading:2842863-Protein Conformation, pubmed-meshheading:2842863-Protein Precursors, pubmed-meshheading:2842863-Protein Processing, Post-Translational, pubmed-meshheading:2842863-Rats, pubmed-meshheading:2842863-Saposins, pubmed-meshheading:2842863-Sphingolipid Activator Proteins, pubmed-meshheading:2842863-Tissue Distribution
pubmed:year
1988
pubmed:articleTitle
Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
pubmed:affiliation
Department of Neurosciences, University of California, San Diego, La Jolla 92093.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't