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Treatment outcome of acute myeloid leukemia (AML) in elderly patients remains unsatisfactory. It has been shown that the infusion of granulocyte colony-stimulating factor-mobilized donor peripheral blood stem cells (G-PBSCs) can enhance graftversus-leukemia effects and speed hematopoietic recovery. Fifty-eight AML patients aged 60-88 years were randomly assigned to receive induction chemotherapy with cytarabine and mitoxantrone (control group; n ‫؍‬ 28) or it plus human leukocyte antigen-mismatched G-PBSCs

Microtransplantation as a postremission therapy may improve outcomes and avoid GVHD in patients with AML-CR1.

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Maize amylose-water suspension (6% w/w) was subjected to single-pass dynamic highpressure microfluidization (DHPM) treatment at 80, 120, 160, and 200 MPa, and changes in the morphology characteristics and physicochemical properties were compared with native maize amylose as a control sample. Laser scattering measurements of particle size demonstrated with microfluidization treatment at 80 MPa showed a slight decrease in mean diameter, while a significant increase was observed above 120 MPa. SEM analysis showed that the surface appearances of maize amylose were altered and the starch granules were partially gelatinized after DHPM treatment. The microfluidization treated maize amylose showed elevated light transmittance and swelling power. However, the solubility was decreased and no significant changes in the freeze-thaw stability. DSC analysis showed a decrease in gelatinization temperatures (T o , T c ) and gelatinization enthalpy (DH) upon highpressure treatment. The texture profile analysis of the starch gel prepared from the suspension treated with high pressure obtained higher hardness and adhesiveness, lower cohesiveness and springiness. The results provide the basic information on the physicochemical properties of maize amylose treated at different microfluidized pressures and indicate the potential possibility of DHPM for starch modification.

Bovine α-lactalbumin (α-LA) is one of major food allergens in cow's milk. The present work sought to research the effects of ultrasonic pretreatment combined with dry heating-induced glycation between α-LA and galactose on the immunoglobulin E (IgE)/immunoglobulin G (IgG)-binding ability and glycation extent of α-LA, determined by inhibition enzyme-linked immunosorbent assay and high-resolution mass spectrometry, respectively. The IgE/IgG-binding ability of glycated α-LA was significantly decreased as a result of ultrasonic pretreatment, while the average molecular weight, incorporation ratio (IR) value, location and number of glycation sites, and degree of substitution per peptide (DSP) value were elevated. When the mixtures of α-LA and galactose were pretreated by ultrasonication at 150 W/cm, glycated α-LA possesses seven glycation sites, the highest IR and DSP values, and the lowest IgE/IgG-binding ability. Therefore, the decrease in the IgE/IgG-binding ability of α-LA depends upon not only the shielding effect of the linear epitope found to be caused by the glycation of K13, K16, K58, K93, and K98 sites but also the intensified glycation extent, which reflected in the increase of the IR value, the number of glycation sites, and the DSP value. Moreover, allergenic proteins and monosaccharides pretreated by ultrasonication and then followed by dry-state glycation were revealed as a promising way of achieving lower allergenicity of proteins in food processing.

Glycation between ovalbumin (OVA) and different monoses under mild dry heating at 37 °C was studied. The content of free amino groups decreased dramatically, and the conformational changes based on fluorescence and circular dichroism spectra were evident in glycated OVA. The glycated sites and the average degree of substitution per peptide molecule per site were determined using liquid chromatography high-resolution mass spectrometry. Lysine and arginine were the predominant glyaction sites, in which Lys207 was a relatively reactive site for glycation in all of the conjugates. In general, the extent of glycation of aldose was higher, and its alterations on the steric layouts of protein were more drastic than those of ketose. The configuration of hydroxyl groups at C-4 in sugar epimers might be important for the glycation reactivity and conformational modification in the glycated proteins. These insights would have important implications for the creation of sweetened food products with desirable structures and excellent quality control.