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1.
Stud Mycol ; 94: 1-124, 2019 Sep.
Article in English | MEDLINE | ID: mdl-31636728

ABSTRACT

This paper represents the third contribution in the Genera of Phytopathogenic Fungi (GOPHY) series. The series provides morphological descriptions, information about the pathology, distribution, hosts and disease symptoms for the treated genera, as well as primary and secondary DNA barcodes for the currently accepted species included in these. This third paper in the GOPHY series treats 21 genera of phytopathogenic fungi and their relatives including: Allophoma, Alternaria, Brunneosphaerella, Elsinoe, Exserohilum, Neosetophoma, Neostagonospora, Nothophoma, Parastagonospora, Phaeosphaeriopsis, Pleiocarpon, Pyrenophora, Ramichloridium, Seifertia, Seiridium, Septoriella, Setophoma, Stagonosporopsis, Stemphylium, Tubakia and Zasmidium. This study includes three new genera, 42 new species, 23 new combinations, four new names, and three typifications of older names.

2.
Exp Physiol ; 85(4): 379-85, 2000 Jul.
Article in English | MEDLINE | ID: mdl-10918077

ABSTRACT

This study was designed to assess the haem-peptide interactions which occur during progressive haemoglobin hydrolysis by digestive enzymes and their relationship with haem iron digestive absorption. The behaviour of different haemoglobin hydrolysates was studied using the Ussing chamber model. Hydrolysates were produced from enzyme digestion of bovine haemoglobin at pH 3 by pepsin and at pH 10 by subtilisin. Samples with increasing degrees of hydrolysis (0-15 %) were studied. Biochemical assays (pyridine haemochromogen method and UV absorption spectra) were used to follow haem solubility and haem-peptide interactions in samples. Increasing the hydrolysis level of haemoglobin was associated with an enhanced iron uptake; the highest uptake rate was reached between 8 and 11 % of globin hydrolysis, whichever enzyme was used. The mechanisms rendering iron soluble and available differ between the two enzymes. The comparison between biochemical and absorption data suggests that the formation of soluble peptide-haem complexes was not sufficient to enhance haem iron absorption, since globin-bound iron is poorly absorbed; an efficient absorption occurred only when haem was loosely bound to low molecular weight peptides.


Subject(s)
Hemoglobins/metabolism , Intestinal Absorption , Iron/metabolism , Pepsin A/metabolism , Subtilisin/metabolism , Animals , Biochemistry/methods , Cattle/blood , Diffusion Chambers, Culture , Female , Hydrogen-Ion Concentration , Hydrolysis , In Vitro Techniques , Iron/blood , Rats , Rats, Sprague-Dawley , Solubility
3.
J Nutr Biochem ; 11(11-12): 562-567, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11137893

ABSTRACT

Previous studies have showed that purified heme iron forms insoluble polymers that are poorly absorbed. The presence of peptides and of amino acids maintaining heme iron in a soluble form could improve its bioavailability. The digestive uptake and transfer of a concentrated hydrolysate of heme peptides (HPH) and of iron gluconate (Gluc) at 100 µM were compared in vitro in a Ussing chamber. The effects of an enhancing amino acid (L-cysteine) on the uptake and transfer of both forms were assessed. An inhibitor of the oxidative phosphorylation (2,4-dinitrophenol; DNP) was used to differentiate the active and passive mechanisms of the absorption. The mucosal uptake (%Tot) and enterocyte transfer (%S) of the two sources of iron did not differ. DNP significantly reduced %Tot and %S of both forms. Cysteine significantly enhanced %Tot and %S of HPH and Gluc, partly corrected the inhibition exerted by DNP on %Tot of HPH and %S of both forms, and fully restored %Tot of Gluc. In presence of peptides produced by globin hydrolysis, the absorption of hemoglobin iron was efficient; it was mostly energy dependent and, therefore, should have occurred by a regulated transcellular pathway. Cysteine enhanced the passive uptake of iron and the passive processes involved in the enterocyte transfer of the common pool made of both sources (heme and nonheme) of iron. These results showed that heme iron can be purified and concentrated without impairing its digestive absorption, provided it remains in presence of peptides or amino acids.

4.
Reprod Nutr Dev ; 38(5): 559-66, 1998.
Article in English | MEDLINE | ID: mdl-9923008

ABSTRACT

We used the Ussing chamber model to study heme iron absorption by rat duodenal mucosa. Heme iron was obtained by enzymic digestion of bovine haemoglobin and concentration of heme (HPH). Its uptake and mucosal transfer was compared to iron gluconate (Gluc), at 100 microM and 1 mM. At 100 microM iron uptake (Qtot), mucosal retention (Qm) and transfer across the mucosa (Qs) was similar for the two sources of iron. Qs was significantly higher at 1 mM for Gluc but not for HPH, and was associated with higher levels of Qm. Addition of L-histidine did not improve iron absorption and indeed it decreased it if iron was provided as Gluc. L-cysteine increased the transfer of iron of both sources. In the in vitro model using rat digestive mucosa, heme iron appeared to be an efficiently used source of iron, which might prevent its accumulation by gut when supplied in excess.


Subject(s)
Amino Acids/pharmacology , Digestion/drug effects , Heme/metabolism , Intestinal Absorption/drug effects , Iron/metabolism , Animals , Cysteine/pharmacology , Duodenum/metabolism , Female , Gluconates/metabolism , Hemoglobins/metabolism , Histidine/pharmacology , Intestinal Mucosa/metabolism , Rats , Rats, Sprague-Dawley
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