The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000
Open accessAbstract
A new method has been developed for purification of cytochrome b from stimulated human granulocytes offering the advantage of high yields from practical quantities of whole blood. Polymorphonuclear leukocytes were treated with diisopropylfluorophosphate, degranulated and disrupted by nitrogen cavitation. Membranes enriched in cytochrome b were prepared by differential centrifugation. Complete solubilization of the cytochrome from the membranes was achieved in octylglucoside after a 1-M salt wash. Wheat germ agglutinin-conjugated Sepharose 4B specifically bound the solubilized cytochrome b and afforded a threefold purification. Eluate from the immobilized wheat germ agglutinin was further enriched by chromatography on immobilized heparin. The final 260-fold purification of the b-type cytochrome with a 20-30% yield was achieved by velocity sedimentation in sucrose density gradients. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the purified preparation revealed two polypeptides of Mr 91,000 and Mr 22,000. Treatment of the 125I-labeled, purified preparation with peptide:N-glycosidase F, which removes N-linked sugars, decreased relative molecular weight of the larger species to approximately 50,000, whereas beta-elimination, which removes O-linked sugars, had little or no effect on the mobility of the Mr-91,000 polypeptide. Neither of the deglycosylation conditions had any effect on electrophoretic mobility of the Mr-22,000 polypeptide. Disuccinimidyl suberate cross-linked the two polypeptides to a new Mr of 120,000-135,000 by SDS-PAGE. Antibody raised to the purified preparation immunoprecipitated spectral activity and, on Western blots, bound to the Mr-22,000 polypeptide but not the Mr-91,000 polypeptide. Western blot analysis of granulocytes from patients with X-linked chronic granulomatous disease revealed a complete absence of the Mr-22,000 polypeptide. These results (a) suggest that the two polypeptides are in close association and are part of the cytochrome b, (b) provide explanation for the molecular weight discrepancies previously reported for the protein, and (c) further support the involvement of the cytochrome in superoxide production in human neutrophils.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“For example, H2O2 can also modulate genes expression by epigenetic modification and activate transcription factors such as AP-1, NRF2, CREB, HSF1, HIF-1, TP53, NF-κβ, NOTCH, SP1, SCREB-1 and FOXO family [14,15,16,17,18,19,20,21,22].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [16]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,218
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
Silver staining of proteins in polyacrylamide gels
Wray, W., Boulikas, T., Wray, V. P., & Hancock, R. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90179-2 · Cited by 3,481
Merril, C. R., Goldman, D. A., Sedman, S. A., & Ebert, M. H. (1981) · Science · doi:10.1126/science.6162199 · Cited by 2,933
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931
Udenfriend, S., Stein, S., Böhlen, P., Dairman, W. M., Leimgruber, W., & Weigele, M. (1972) · Science · doi:10.1126/science.178.4063.871 · Cited by 2,639
Active Oxygen Species and the Functions of Phagocytic Leukocytes
Badwey, J. A., & Karnovsky, M. L. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.003403 · Cited by 1,110
Borregaard, N., Heiple, J. M., Simons, E. R., & Clark, R. A. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.1.52 · Cited by 920
Cited by
Sorted by citations
Items 401–454 of 454
Antimicrobial Activity of Leukocytes
BABIOR, B. M., Hoyal, C. R., Lehrer, R. I., & Ganz, T. (2001) · Springer eBooks · doi:10.1007/978-1-4614-7512-5_10 · Cited by 3
Levine, A. P., & Segal, A. W. (2017) · ASM Press eBooks · doi:10.1128/9781555819194.ch33 · Cited by 1
Riesselman, M. H., & Jesaitis, A. J. (2014) · Methods in molecular biology · doi:10.1007/978-1-62703-845-4_24 · Cited by 2
Self-citationRogers, C. B. (2009) · Cited by 2
Tomizawa, K., Sakiyama, Y., Matsumoto, S., & Nakamura, M. (1991) · European Journal Of Haematology · doi:10.1111/j.1600-0609.1991.tb00516.x · Cited by 2
The Discovery and Characterisation of Nox2, a Personal Journey
Segal, A. W. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_4 · Cited by 1
Die NADPH-Oxidase im Gefäßsystem
Ushio‐Fukai, M. (2001) · Steinkopff eBooks · doi:10.1007/978-3-642-87803-9_6 · Cited by 1
Čepica, S., Musilová, P., Stratil, A., Juráková, M., & Rubeš, J. (1997) · Mammalian Genome · doi:10.1007/s003359900424 · Cited by 1
Sakashita, A., Curnutte, J. T., & Koeffler, H. P. (1994) · British Journal of Haematology · doi:10.1111/j.1365-2141.1994.tb04973.x · Cited by 1
Polymorphonuclear leukocytes in acute inflammation
Jones, O. T. G., & Cross, A. R. (1988) · Springer eBooks · doi:10.1007/978-94-009-1293-9_1 · Cited by 1
Segal, A. W., & Nugent, J. H. A. (1992) · Elsevier eBooks · doi:10.1016/b978-0-12-150404-5.50005-2 · Cited by 1
The Neutrophil Respiratory Burst Oxidase
Quinn, M. T. (2013) · IMPERIAL COLLEGE PRESS eBooks · doi:10.1142/9781848168374_0002 · Cited by 1
Chronic Granulomatous Disease of Childhood
Ambruso, D. R., & Johnston, R. B. (2006) · Elsevier eBooks · doi:10.1016/b978-0-7216-3695-5.50073-0 · Cited by 1
Corey, S. J., & Rosoff, P. M. (1989) · Springer eBooks · doi:10.1007/978-94-009-1279-3_2 · Cited by 1
Kuwabara, W. M. T. (2013) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.42.2013.tde-23052014-101531
NADPH oxydase Nox4 : structure/fonction protéomique recombinante et approche immunologique
Zhang, L. (2011) · theses.fr (ABES) · doi:10.70675/6253c341z0c22z4fddzbc8bzda43aae95e65
The Role of Macrophages in Regulating Inflammation by Oxidative Burst
Pizzolla, A. (2011)
Eixo IL-12/23-IFN-g e o sistema NADPH oxidase.
Aragão-Filho, W. C. (2014) · doi:10.11606/t.42.2014.tde-24092014-201608
Efeito do IFN-k e TNF-α sobre a expressão gênica de CYBB e processamento de seus transcritos.
Frazão, J. B. (2014) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2014.tde-11072014-104454
Domachowske, J. B. (1995) · Clinical Microbiology Newsletter · doi:10.1016/0196-4399(95)80036-0
Ouml, S. E. A., zbabacan, Tekir, S. D., Ouml, K., uuml, & lgen (2011) · International Journal of the Physical Sciences · doi:10.5897/ijps11.109
The oxidative metabolism by eosinophils : Effects of allergen exposure and interleukin-5
Woschnagg, C. (2000) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Age-Related ENOX Proteins (arNOX)
Morré, D. J., & Morré, D. M. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3958-5_9
EFEITO DO IFN- E TNF- SOBRE A EXPRESSÃO GÊNICA DE CYBB E PROCESSAMENTO DE SEUS TRANSCRITOS
Imunologia, G. E. (2014)
Genetic Defects of Phagocyte Nadph Oxidase Activity and Activation
Bellavite, P., Bazzoni, F., Scolaro, G., Poli, G., Dusi, S., & Cassatella, M. A. (1989) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463208900200204
Paulo, S., & Humana, F. (2013)
In search for novel agents in therapy of Plasmodium falciparum
Mathematisch-naturwissenschaftlichen Fakultät, I. (2007)
THE COMPONENTS OF THE RESPIRATORY BURST OXIDASE OF HUMAN NEUTROPHILS
BABIOR, B. M. (1991) · Elsevier eBooks · doi:10.1016/b978-0-08-041749-3.50118-2
Bibliography Articles Cited in Commentaries
Lichtman, M. A., Spivak, J. L., Boxer, L. A., Shattil, S. J., & HENDERSON, E. (2000) · Elsevier eBooks · doi:10.1016/b978-012448510-5/50184-9 · Cited by 1
ioche istry an Molecular iology of Chronic Granulo atous Disease
Segal, A. W. (1992)
Marroushi, Z. (2017) · The Atrium (University of Guelph)
The NADPH oxidase-induced phagosomal environment of neutrophils and other phagocytes
Foote, J. R. (2019) · UCL Discovery (University College London)
Nox protein expression, purification and structure analysis
Baniulis, D. (2004) · Montana State University ScholarWorks (Montana State University)
p40-phox, a novel cytosolic component of neutrophil NADPH oxidase.
Someya, A. (1998) · Ensho · doi:10.2492/jsir1981.18.181
Prospects for Gene Therapy of Inherited Immunodeficiency
Casimir, C. M. (1999) · Blood cell biochemistry · doi:10.1007/978-1-4615-4889-8_6
Physiological Functions and Pathological Significance of NADPH Oxidase 3
Nakano, Y., & Bánfi, B. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_11
Tools to Identify Noxes and their Regulators
Schröder, K. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_19
EROS protein: Decoding its pivotal role in redox homeostasis and disease pathogenesis
Liang, S., Zhou, Y., Ren, W., Xu, Y., Tang, M., Su, Y., Li, L., & Gao, M. (2025) · Advances in Redox Research · doi:10.1016/j.arres.2025.100147
Susceptibilité mendélienne aux maladies infectieuses chez l'homme : déficits en NEMO et NRAMP1
Hubeau, M. (2013) · theses.fr (ABES) · doi:10.70675/3a76475dz8fbdz46b9z8759z2e9f0feaa160
Caractérisation structurale et fonctionnelle de SpNox, une NADPH oxydase bactérienne
Vermot, A. (2020) · theses.fr (ABES) · doi:10.70675/8982dcf6zda88z4163z9743z5b4415e9889f
Pesenti, L. (2024) · theses.fr (ABES) · doi:10.70675/04a80eeazdd63z42e4zbd7fz230cf5dbc199
EROS, a Crucial Regulator of NOX2: Past, Present, and Future
Thomas, E. K., & Thomas, D. (2026) · Springer eBooks · doi:10.1007/978-3-032-21135-4_11
Falling in Love with Nox2: My Journey to Ithaka (A Scientific Autobiography)
Pick, E. (2026) · Springer eBooks · doi:10.1007/978-3-032-21135-4_1
Rochas, P., Val-Pevida, M., Beaumel, S., Petit-Härtlein, I., Plazy, C., Fieschi, F., & Stasia, M. J. (2026) · Antioxidants · doi:10.3390/antiox15060724
Liu, Y., Chi, Y., Yin, J., & Yao, J. (2026) · PLoS ONE · doi:10.1371/journal.pone.0360537
The interaction of UVA radiation with cultured human skin cells
Zhang, J. (2014) · The University of Bath Online Publications Store (The University of Bath)
Metadata
- Authors
- Parkos, C. A., Allen, R. A., Cochrane, C. G., & Jesaitis, A. J.
- Affiliations
- Scripps Research Institute (US)
- Venue
- Journal of Clinical Investigation
- Published
- 1987-09-01
- Volume
- 80
- Issue
- 3
- Pages
- 732-742
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC442297
- OpenAlex
- W2143908574
- Cited by
- 455
- References
- 51
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 5 · 2023: 5 · 2022: 2 · 2021: 4 · 2020: 2 · 2019: 4 · 2018: 4 · 2017: 6 · 2016: 3 · 2015: 5 · 2014: 12 · 2013: 12 · 2012: 6
- FWCI
- 12.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- U.S. Public Health Service (RR 00833)
- National Institute of Allergy and Infectious Diseases (AI17354, R0I AI 22735)
- National Center for Research Resources (RR-00833)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- human granulocytes, polymorphonuclear leukocytes, plasma membrane, N-glycosylation, X-linked chronic granulomatous disease, diisopropylfluorophosphate, wheat germ agglutinin affinity chromatography, leukocyte membrane
- MeSH terms
- Antibodies, Cell Membrane, Cross-Linking Reagents, Cytochrome b Group, Glycosylation, Granulocytes, Humans, Immunologic Techniques, Molecular Weight, Peptides
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
