Mass Spectrometry is a peer-reviewed, open access journal publishing articles in all areas of mass spectrometry. Published continuously online, the journal is fully indexed in J-STAGE and PubMed Central.
Mass Spectrometry welcomes submissions from around the world.

About the journal

Mass Spectrometry is an academic journal on both fundamentals and applications of mass spectrometry, owned and published by the Mass Spectrometry Society of Japan (MSSJ).

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Anyone may access all articles in Mass Spectrometry from J-STAGE and PMC.



This site is operated by the Mass Spectrometry Society of Japan.

The Mass Spectrometry Society of Japan
c/o Academy Center, Yamabuki-cho 358-5, Shinjuku-ku, Tokyo 162-0801, Japan
TEL: +81-3-6824-9378
E-mail: mssj-post[at]
(Note : change [at] to @ when typing in address.)

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Latest articles

Technical ReportMarch 26, 2024

Skin dryness and irritant contact dermatitis induced by the prolonged use of surgical gloves are issues faced by physicians. To address these concerns, manufacturers have introduced surgical gloves that incorporate a moisturizing component on their inner surface, resulting in documented results showing a reduction in hand dermatitis.

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ReviewFebruary 27, 2024

Among the most typical posttranslational modifications is glycosylation, which often involves the covalent binding of an oligosaccharide (glycan) to either an asparagine (N-linked) or a serine/threonine (O-linked) residue. Studies imply that the N-glycan portion of a glycoprotein could serve as a particular disease biomarker rather than the protein itself because N-linked glycans have been widely recognized to evolve with the advancement of tumors and other diseases.

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Original ArticleFebruary 23, 2024

The collision-induced dissociation (CID) behaviors of protonated molecules of anabaenopeptins, a group of cyanobacterial cyclic peptides, were investigated in detail using liquid chromatography-tandem mass spectrometry. Although anabaenopeptin A and B share a macrocyclic peptide structure, they give strikingly different fragmentation patterns; the former gives a variety of product ions including cleavages in the cyclic peptide structure, which is useful for structural analysis; whereas the latter gives far fewer product ions and no fragmentation in the cyclic moiety.

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