Structural Differences between the Nanocrystalline Soft Magnetic Fe73.5Si13.5B9Nb3Cu1and Fe86Zr7B6Cu1Alloys

Oxide phases having the hollandite structure have been identified in multiphase ceramic waste forms being developed for radioactive waste disposal. High resolution studies of phases in the waste forms described in Ref. [2] were initiated to examine them for fine scale structural differences compared to natural mineral analogs. Two hollandites were studied: a (Ba,Cs,K)-titan-ate with minor elements in solution that is produced in the waste forms, and a synthesized BaAl2Ti6O16 phase containing ∼ 4.7 wt% Cs2O. Both materials were consolidated by hot pressing at temperatures above 1100°C. Samples for high resolution microscopy were prepared both by ion-milling (7kV argon ions) and by crushing and dispersing the fragments on holey carbon substrates. The high resolution studies were performed in a JEM 200CX/SEG operating at 200kV.

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Microstructure in soft magnetic E3 (S1, Al) (Sendust) alloys

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100105916 ◽

1988 ◽

Vol 46 ◽

pp. 770-771

Author(s):

June D. Kim

Keyword(s):

Electron Microscopy ◽

Magnetic Properties ◽

Ternary Phase Diagram ◽

Vertical Tube ◽

Vacuum Induction Melting ◽

Induction Melting ◽

Soft Magnetic ◽

Quenching Temperature ◽

Thin Foils ◽

Vertical Tube Furnace

Iron-base alloys containing 8-11 wt.% Si, 4-8 wt.% Al, known as “Sendust” alloys, show excellent soft magnetic properties. These magnetic properties are strongly dependent on heat treatment conditions, especially on the quenching temperature following annealing. But little has been known about the microstructure and the Fe-Si-Al ternary phase diagram has not been established. In the present investigation, transmission electron microscopy (TEM) has been used to study the microstructure in a Sendust alloy as a function of temperature.An Fe-9.34 wt.% Si-5.34 wt.% Al (approximately Fe3Si0.6Al0.4) alloy was prepared by vacuum induction melting, and homogenized at 1,200°C for 5 hrs. Specimens were heat-treated in a vertical tube furnace in air, and the temperature was controlled to an accuracy of ±2°C. Thin foils for TEM observation were prepared by jet polishing using a mixture of perchloric acid 15% and acetic acid 85% at 10V and ∼13°C. Electron microscopy was performed using a Philips EM 301 microscope.

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Soft Magnetic Properties of Fe-Ti-N Alloy Thin Films

Journal of the Magnetics Society of Japan ◽

10.3379/jmsjmag.22.186 ◽

1998 ◽

Vol 22 (4_1) ◽

pp. 186-189

Author(s):

M. Matsumoto ◽

A. Morisako ◽

Y. Mutoh

Keyword(s):

Thin Films ◽

Magnetic Properties ◽

Soft Magnetic Properties ◽

Soft Magnetic

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CHEMISTRY OF GONADOTROPHINS IN RELATION TO THEIR ANTIGENIC PROPERTIES

Acta Endocrinologica ◽

10.1530/acta.0.062s013 ◽

1969 ◽

Vol 62 (1_Suppl) ◽

pp. S13-S30 ◽

Cited By ~ 8

Author(s):

W. R. Butt

Keyword(s):

Biological Activity ◽

Guinea Pigs ◽

Complement Fixation ◽

Neuraminic Acid ◽

Fixation Technique ◽

Immunological Activity ◽

Antigenic Properties ◽

Specific Antisera ◽

Structural Differences

ABSTRACT Several chemical differences between FSH, LH and HCG have been reported: thus LH and HCG are richer in proline than FSH and FSH and HCG contain more N-acetyl neuraminic acid than LH. Sub-units of LH are formed by treatment with urea, guanidine or acid. HCG also may contain two sub-units. The sub-units from LH are biologically inert but retain their immunological activity: biological activity is restored when the sub-units are incubated together. There is much evidence from chemical and enzymic reactions that antigenic groups are distinct from those parts of the molecule essential for biological activity. N-acetyl neuraminic acid and probably other carbohydrates in FSH and HCG are not involved in immunological activity but are necessary for biological activity. Histidine, methionine and possibly cysteine appear to be essential for biological but not immunological activity of FSH, while tryptophan and possibly tyrosine are not essential for either. A few highly specific antisera to gonadotrophins have been prepared in rabbits and guinea pigs to crude antigens: there is no evidence that purified antigens are more likely to produce specific antisera. Differences in the immunological reactivities of urinary compared with pituitary gonadotrophins have been observed both by radioimmunoassay and by the complement fixation technique. The latter may be particularly useful for detecting structural differences in the hormones.

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