Crosslinking of low-affinity glycoprotein ligands to galectin LEC-1 using a photoactivatable sulfhydryl reagent

2006 ◽  
Vol 350 (1) ◽  
pp. 185-190 ◽  
Author(s):  
Yoichiro Arata ◽  
Mayumi Tamura ◽  
Takamasa Nonaka ◽  
Ken-ichi Kasai
Keyword(s):  
Sulfhydryl Reagent

scholarly journals N-(3-Pyrene)maleimide: a Long Lifetime Fluorescent Sulfhydryl Reagent

1973 ◽  
Vol 248 (9) ◽  
pp. 3173-3177
Author(s):  
Joel K. Weltman ◽  
Robert P. Szaro ◽  
A. Raymond Frackelton ◽  
Robert M. Dowben ◽  
James R. Bunting ◽  
...  
Keyword(s):  
Sulfhydryl Reagent ◽  
Long Lifetime

CHARACTERIZATION OF HUMAN OVARIAN OESTRADIOL-17β OXIDOREDUCTASE ACTIVITY

1977 ◽  
Vol 85 (3) ◽  
pp. 624-635 ◽  
Author(s):  
Donald E. Pittaway ◽  
Richard N. Andersen ◽  
James R. Givens
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Enzyme Preparation ◽  
Phenolic Hydroxyl ◽  
Supernatant Fraction ◽  
Oxidoreductase Activity ◽  
Sulfhydryl Reagent ◽  
Michaelis Constants ◽  
Human Ovaries

ABSTRACT Oestradiol-17β oxidoreductase activity, which catalyzes the interconversion of oestrone and oestradiol, was investigated in preparations of human ovaries. The enzyme activities were localized primarily in the 105 000 × g supernatant fraction; dialyzed supernatant preparations were used in subsequent studies. The pH optima were 6.9 for reduction and 8.1 for 17β-dehydrogenation. The apparent Michaelis constants for oestrone and oestradiol were 1 × 10-7 m and 5 × 10-7 m, respectively. The enzyme activity was present with either NADP(H) or NAD(H), though NADP(H) were the preferred cofactors. Non-aromatic steroids androstenedione, dehydroepiandrosterone, testosterone and 5-androstene-3β,17β-diol were poor substrates for the enzyme preparation. Methylation of the phenolic hydroxyl of oestrone and oestradiol resulted in slightly enhanced activities. The sulfhydryl reagent, N-ethylmaleimide, inhibited the reduction of oestrone. A dialyzed supernatant preparation retained approximately 79 % of the original enzyme activity when stored at −20°C for 6 weeks.

Olfactory Bulbar Electrical Responses of Rainbow Trout (Salmo gairdneri) Exposed to Morpholine During Smoltification

1979 ◽  
Vol 36 (10) ◽  
pp. 1186-1190 ◽  
Author(s):  
Toshiaki J. Hara ◽  
S. B. Brown
Keyword(s):  
Rainbow Trout ◽  
Key Words ◽  
Electrical Response ◽  
Salmo Gairdneri ◽  
Induced Responses ◽  
Salmonid Fishes ◽  
Key Words Olfaction ◽  
Sulfhydryl Reagent ◽  
Significant Difference ◽  
Olfactory Organs

Exposure of rainbow trout (Salmo gairdneri) to 5.7 × 10−10 M (5 × 10−5 mg/L) morpholine during smoking period did not influence the subsequent neural response to this substance, when tested immediately and 12 mo after smoking. No significant difference in the morpholine-induced responses was obtained between the exposed and unexposed fish. Using N-ethylmaleimide, a sulfhydryl reagent, it was further confirmed that the morpholine-effect is caused by a mechanism not directly associated with the normal olfactory function. Perfusion of the olfactory organs with 1.0 × 10−1 and 1.1 × 10−1 M (1%) morpholine for 10 min irreversibly inhibited the olfactory responsiveness to odorants. Sensitization of the olfactory bulbar electrical response is discussed in connection with homing of morpholine-imprinted salmonid fishes. Key words: olfaction, olfactory bulbar response, rainbow trout, salmon, imprinting, morpholine, homing, migration

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