Influence of Konjac Glucomannan on the Crystallization Morphology and Structure of Calcium Oxalate

The influence of additive Konjac Glucomannan （KGM） in a variety of con- centrations on the crystallization morphology and structure of calcium oxalate （CaOxa） has been investigated by infrared spectroscopy, scanning electron microscope, X-ray diffraction and so on. The results showed KGM can complex with the Ca^2＋ ions; low concentration KGM prevents CaOxa from aggregating, raises the concentration of ions in the solution, reduces the quantity of crystals and inhibits their growth, and the crystals are round and blunt; while high concentration KGM promotes the growth of crystal, which appears in sheet-like or irregular shape. Only CaOxa monohydrate was observed in a certain system with or without the presence of KGM.

Studies on the Molecular Chain Conformation Stability of Aminated Konjac Glucomannan

Konjac glucomannan （KGM） was aminated by 2-chloroethyl-amine （CEA） as reagent so as to study the influence of concentration of CEA （based on the amount of KGM）, concentration of NaOH, reaction time and temperature on the extent of amination. And the molecular simulation technology was adopted to analyze the conformation stability of aminate （AKGM）. The results indicate that when the amount of CEA is higher, the extent of amination is higher. The optimum concentration of NaOH, reaction time and temperature are 10% NaOH, 70 ℃ and 45 rain, respectively. IR shows KGM is successfully aminated. The conformation of AKGM is in a random clew-like shape.

Studies on the Hydrogen Bonding Network Structures of Amino-konjacglucomannan-zinc Chelate

Amino-Konjacglucomannan （NH2-KGM） was prepared through the reaction of ammonium hydroxide with KGM by ultrasonic. The influence of amount of ammonium hydroxide, concentration of KGM and ultrasonic time on the extent of amination was studied. Then, NH2-KGM and zinc sulfate were used as materials for the preparation of NH2-KGM-Zn complex. The results indicated that the extent of amination increases with increasing the ammonium hydroxide. The optimum concentration of KGM and ultrasonic time are 0.3% and 75 rain respectively. IR showed KGM is successfully aminated and NH2-KGM forms stable complex with zinc（II ）. The hydrogen bonding network structures of NH2-KGM-Zn are more stable and the key linking points of hydrogen bonding network are at the OH（6） and 0（3） positions of mannose and OH（2） of glucose and 0（3） of mannose on the KGM ring. It is more favorable for NH2-KGM-Zn to form intermolecular hydrogen bonds between KGM.

Expression pattern and regulation of head-to-head genes Vps36 and Ckap2 during chicken follicle development

Vacuolar protein sorting 36(VPS36),a protein primarily known for its role in the Endosomal Sorting Complex Required for Transport pathway,has recently been shown to be linked to chicken reproduction.Previous research showed that Vps36 is significantly downregulated in sexually mature chicken ovaries compared to immature ones.In this study,using real-time quantitative RT-PCR,we investigated the expression pattern of Vps36 and its head-to-head gene Ckap2 mRNA in chicken follicles.Small white follicles were found to have significantly higher expression of Vps36 and Ckap2 mRNA than any other sized follicles(P<0.05).The expression of Vps36 and Ckap2 mRNA were detected in both granulosa and theca layers of pre-ovulatory follicles,the expression of Ckap2 in theca layers was slightly higher than in granulosa cells.Treatment of small yellow follicles with folliclestimulating hormone and estradiol resulted in a marked decrease of both Vps36 and Ckap2 mRNA(P<0.05);however,progesterone,transforming growth factor-β1 and luteinizing hormone induced no significant changes in Vps36 and Ckap2 mRNA expression in these follicles.These results indicate that the head-to-head genes of Vps36 and Ckap2 exhibit similar expression in chicken follicles and are involved in chicken follicle development.