ArticleThe Biochemical journal1986
Determination of the molecular mass of apolipoprotein B-100. A chemical approach.
Article in The Biochemical journal, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Century of Progress on the Structure of APOB-100 in Atherogenic Lipoproteins.Circulation research · 2026Review
- Lipoprotein(a), apolipoprotein B and other lipid biomarkers in Asian healthcare workers.Lipids in health and disease · 2026Article
- LDL-Bound PCSK9 Has a Slower Clearance Kinetic and Higher Use for HSPGs Than Free-PCSK9-Brief Report.Arteriosclerosis, thrombosis, and vascular biology · 2025Article
- Lipoprotein(a) and risk-weighted apolipoprotein B: a novel metric for atherogenic risk.Lipids in health and disease · 2024Article
- 10th International Conference on Methods in Protein Structure Analysis. September 8-13, 1994, Snowbird, Utah. Short communications and abstracts.Journal of protein chemistry · 1994Article
- Apolipoproteins and metabolism in atherosclerosis.Transactions of the American Clinical and Climatological Association · 1990Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Apolipoprotein B-100 (apo B-100) is the protein ligand in low-density lipoproteins that binds to a specific cell-surface receptor. Its molecular mass has been a subject of controversy. We have determined the molecular mass of the protein by a chemical approach. After complete CNBr cleavage, the C-terminal fragment of apo B-100 was purified by reverse-phase h.p.l.c. Amino acid N- and C-terminal analyses confirm that this peptide represents the C-terminal peptide as deduced from the DNA sequence of a human apo B-100 cDNA clone. A chemically synthesized peptide was used to determine the recovery of the peptide (74.72%). On the basis of these data, the molecular mass of apo B-100 was determined to be 496.82 +/- 24.84 kDa.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.