Demonstration of needle-shaped hepatic inclusions in porphyria cutanea tarda using the ferric ferricyanide reduction test

1987 ◽  
Vol 411 (4) ◽  
pp. 365-368 ◽  
Author(s):  
Franti?ek Fakan ◽  
Alena Chlumsk�
1941 ◽  
Vol 24 (4) ◽  
pp. 399-421 ◽  
Author(s):  
M. L. Anson

1. 1 cc. of 0.001 M ferricyanide, tetrathionate, or p-chloromercuribenzoate is required to abolish the SH groups of 10 mg. of denatured egg albumin in guanidine hydrochloride or Duponol PC solution. Both the nitroprusside test and the ferricyanide reduction test are used to show that the SH groups have been abolished. 2. 1 cc. of 0.001 M ferrocyanide is formed when ferricyanide is added to 10 mg. of denatured egg albumin in neutral guanidine hydrochloride or urea solution. The amount of ferricyanide reduced to ferrocyanide by the SH groups of the denatured egg albumin is, within wide limits, independent of the ferricyanide concentration. 3. Ferricyanide and p-chloromercuribenzoate react more rapidly than tetrathionate with the SH groups of denatured egg albumin in both guanidine hydrochloride solution and in Duponol PC solution. 4. Cyanide inhibits the oxidation of the SH groups of denatured egg albumin by ferricyanide. 5. Some samples of guanidine hydrochloride contain impurities which bring about the abolition of SH groups of denatured egg albumin and so interfere with the SH titration and the nitroprusside test. This interference can be diminished by using especially purified guanidine hydrochloride, adding the titrating agent before the protein has been allowed to stand in guanidine hydrochloride solution, and carrying out the nitroprusside test in the presence of a small amount of cyanide. 6. The SH groups of egg albumin can be abolished by reaction of the native form of the protein with iodine. It is possible to oxidize all the SH groups with iodine without oxidizing many of the SH groups beyond the S-S stage and without converting many tyrosine groups into di-iodotyrosine groups. 7. p-chloromercuribenzoate combines with native egg albumin either not at all or much more loosely than it combines with the SH groups of denatured egg albumin or of cysteine. 8. The compound of mercuribenzoate and SH, like the compound of aldehyde and SH and like the SH in native egg albumin, does not give a nitroprusside test or reduce ferricyanide but does reduce iodine.


1953 ◽  
Vol 1 (2) ◽  
pp. 87-92 ◽  
Author(s):  
R. D. LILLIE ◽  
HELEN J. BURTNER

Ascorbic, oxalic and uric acids, phenols, indols, pyrrols, aryl amines, hydrazines, thiols and inorganic sulfides and peroxide promptly reduce ferric ferricyanide mixtures to Prussian blue. Most of the other substances tested reacted feebly or slowly, and probably need not be considered in the histochemical test, provided the reaction time is kept down to 10 to 15 minutes.


Author(s):  
Rodolfo E. Vallejos ◽  
Jesus Vivas

Lately we have reported keratohyalin bodies of nuclear origin in the flat superficial cells of bovine ruminal epithelium; apparently this origin is based on a chromatin condensation, which includes light inner vacuoles, acquiring a spherical or semilunar shape. In order to demonstrate the keratohyalin content in these bodies, we have adapted the Chévremont & Fréderic ferric ferricyanide test - for proteins containing thiol groups - to the electron microscope histochemistry.Biopsies of ruminal papillae were taken from three adult bovines, few minutes after their sacrifice; small samples of tissue were fixed during four hours in cold 2.5% formaldehyde and 0. 2 M cacodylate buffer at pH 7.4. After fixation, the tissue blocks were rinsed overnight at 4°C in several changes of 0.2 M cacodylate buffer containing 0.22 M sucrose.


Author(s):  
Veronika Burmeister ◽  
R. Swaminathan

Porphyria cutanea tarda (PCT) is a disorder of porphyrin metabolism which occurs most often during middle age. The disease is characterized by excessive production of uroporphyrin which causes photosensitivity and skin eruptions on hands and arms, due to minor trauma and exposure to sunlight. The pathology of the blister is well known, being subepidermal with epidermodermal separation, it is not always absolutely clear, whether the basal lamina is attached to the epidermis or the dermis. The purpose of our investigation was to study the attachment of the basement membrane in the blister by comparing scanning with transmission electron microscopy.


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