A search for the rare decay K L → π 0 νν was performed. With the data collected in 2015, corresponding to 2.2 × 10 19 protons on target, a single event sensitivity of ð1.30 AE 0.01 stat AE 0.14 syst Þ × 10 −9 was achieved and no candidate events were observed. We set an upper limit of 3.0 × 10 −9 for the branching fraction of K L → π 0 νν at the 90% confidence level (C.L.), which improved the previous limit by almost an order of magnitude. An upper limit for K L → π 0 X 0 was also set as 2.4 × 10 −9 at the 90% C.L., where X 0 is an invisible boson with a mass of 135 MeV=c 2 .

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A serum lectin specific for mannose and N-acetylglucosamine residues was isolated from human serum to near homogeneity mainly by affinity chromatography on a column of Sepharose 4B-mannan. The lectin, called mannan-binding protein, was a glycine-rich protein with an apparent molecular size of approximately 600,000 daltons, and had a subunit structure consisting of a single component with an apparent molecular weight of 31,000. Binding of the isolated lectin to 125I-labeled mannan was dependent upon the presence of Ca2+, proportional to the protein added, and a reversible and saturable process. Scatchard plot analysis of binding data indicated the presence of a binding site with a dissociation constant of 2.3 X 10(-9) M and a maximum capacity of 4.3 pmol of 125I-labeled mannan per microgram of protein (2.6 mol of mannan per mol of the protein). The mannan-binding protein, is different from C-reactive protein (CRP) and amyloid P-component (SAP), both of which are serum components known to bind polysaccharides in the presence of Ca2+. A distinct binding activity toward mannan which did not require Ca2+ was attributed to immunoglobulins (IgG).

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