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At least 217 records · Page 12Linked to original sources
PubMed1989

Plant protein rehabilitation diets and iron supplementation of the protein-energy malnourished child.

Thirty-eight children admitted to the paediatric ward of Obafemi Awolowo University Teaching Hospital, Ile-Ife, were treated using a local therapeutic regimen for protein-energy malnutrition (PEM). Serum transferrin concentration was measured at weekly intervals to determine the response to and nutritional adequacy of the dietary component of this therapeutic regimen. At discharge, weight for height measurements in the children showed a significant (P less than 0.001) increase in growth although the expected weight for height was not attained. Serum transferrin concentration rose significantly from a mean basal level of 132.1 +/- 17.2 mg/dl to 222.0 +/- 24.6 mg/dl at the end of the first week of hospitalization and at discharge was 403.2 +/- 27.8 mg/dl. Although not statistically significant, mortality was highest amongst children for whom iron supplementation started early on admission. Earlier studies on the aetiology and treatment of anaemia in PEM have argued in favour of routine treatment with iron to prevent the development of anaemia during the recovery phase, but data from this study suggest that iron therapy should not be instituted during the first week of treatment.

Anemia, Hypochromic↗
PubMed2004

The plant uncoupling protein homologues: a new family of energy-dissipating proteins in plant mitochondria.

Uncoupling proteins (UCPs) form a subfamily within the mitochondrial carrier protein family, which catalyze a free fatty acid-mediated proton recycling and can modulate the tightness of coupling between mitochondrial respiration and ATP synthesis. As in mammalian tissues, UCPs are rather ubiquitous in the plant kingdom and widespread in plant tissues in which they could have various physiological roles, such as heat production or protection against free oxygen radicals. The simultaneous occurrence in plant mitochondria of two putative energy-dissipating systems, namely UCP which dissipates the proton motive force, and alternative oxidase (AOX) which dissipates the redox potential, raises the question of their functional interactions.

Carrier Proteins↗
PubMed1978

[Lectins, sugar-binding plant proteins].

Lectins are proteins which can bind to the surfaces of animal and human cells. They are widespread in the plant and animal kingdom. Though many lectins have been isolated and characterized, and though some are extensively used as cell surface "tools", their biological role is only subject to hypotheses.

Animals↗
PubMed1990

Light as a signal influencing the phosphorylation status of plant proteins.

The phosphorylation-status of a number of plant enzymes has been shown to be altered in response to light. Phosphoenolpyruvate carboxylase is phosphorylated (more active) in C(4) plants in the light but CAM phosphoenolpyruvate carboxylase is phosphorylated (more active) in the dark. C(4) plant pyruvate, Pi dikinase is dephosphorylated (activated) in the light and sucrose phosphate synthase is less phosphorylated (more active) in the light. The mitochondrial pyruvate dehydrogenase is inactivated (phosphorylated) in the light. The reversal of these events occurs in the dark or when photosynthesis is inhibited. Phytochrome and blue light receptors also alter the phosphorylation-status of proteins. The evidence is rapidly increasing in support of signal transduction networks in plants that involve light reception.

Journal Article↗
PubMed1990

Sequence analysis of arcelin 2, a lectin-like plant protein.

The nucleotide sequence of the cDNA clone encoding arcelin 2 (Arc2), one member of a family of closely related lectin-like plant toxins from wild bean accession, is presented. The sequence contains a 265-amino acid (aa) open reading frame and is 99.3% homologous to Arc1, another of the four electrophoretic variants with proven antibiosis characters. These two proteins differ by four aa residues. Based on cross hybridizations of RNAs, it is assumed that Arc4 is more divergent than Arc1 and Arc2. Furthermore, it is likely that at least three of the variants are polypeptides of similar size and the observed molecular weight differences between them are due to differences in the number of glycosylation sites.

Amino Acid Sequence↗
PubMed1984

[Effect of the content of crude plant protein in feed on the utilization of urea in dairy cattle. 4. Passage of amino acids through the duodenum].

Model investigations carried out by means of a re-entrant method at the duodenum with dairy cows and with energy-equivalent rations (600 EFU cattle/kg DM), which after the supplementation of 11 g urea/kg DM (150 g/animal and day) contained 13.8 (I), 16.7 (II) and 20.2 (III)% crude protein, had the following results: The amino acid profile of the duodenal protein differed from that of the applied rations and was similar to the microbial protein in the rumen. It only changed inconsiderably with the protein level of the ration. There were differences between the amino acids of the feed as to their apparent rate of fermentation in the rumen. Ser, tyr, lys, and leu apparently proved to be most resistent whereas arg, asp, met, ile and phe were apparently fermented for the most part or completely. The passage rate of amino acids at the duodenum related to intake were, from I ... III 126, 102 and 87%. With all rations there were always net losses of some amino acids (his, arg) and net gains (lys, thr, ser, gly, val, met and tyr) at the duodenum in comparison intake. 15N from urea was incorporated into all the amino acids determined in the duodenal protein, most intensively into glu, ser, asp, ile, gly, his and leu. The apparent digestibility of the total amino acids in the intestines was independent of the crude protein level of the rations and reached 69 ... 71% with a deviation range of 59 ... 81% for the individual amino acids.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗
PubMedDate not supplied

[Effect of diets containing plant protein on liver mono-oxygenase activity in rats].

Male Wistar rats kept for 30 days on the diet containing vegetative (wheat) protein demonstrate an increase in cytochrome P-450 concentration in liver microsomes and an increase in the rate of amidopyrine N-demethylation and aniline p-hydroxylation. Administration of phenobarbital leads to cytochrome P-450 induction and activation of monooxygenase of rat liver microsomes, the quality of food protein not affecting cytochrome induction. It is assumed that high content of cytochrome P-450 is linked with prolongation of the time of cytochrome P-450 renewal at the expense of the decreased constant of its protein part degradation or with activation of cytochrome synthesis de novo (based on the preliminary data).

Aminopyrine N-Demethylase↗
PubMed2002

Analysis of putative interactions between potyviral replication proteins and plant retinoblastoma proteins.

Sequence comparisons suggest that the RNA-dependent RNA polymerase (NIb) of potyviruses and bymoviruses, as well as the viral polymerase of potexviruses may contain a putative retinoblastoma protein (pRb) binding motif. The possibility that the potyviral NIb may function in the nucleus through interactions with plant pRb-related (RBR) proteins, and the modifications of the cell cycle was investigated by a combination of mutagenesis of the NIb and yeast two-hybrid system (YTHS). Mutation of a highly conserved glutamic acid residue in the putative pRb-binding motif of the NIb had no detectable phenotypic effect on replication of Potato virus A (PVA). Furthermore, the NIb proteins from Potato virus V and PVA failed to interact with maize or tobacco RBR proteins in yeast. Although the conservation of the motif for pRb interaction in plant RNA viruses is intriguing, these proteins from plant RNA viruses appear not to interact with plant RBR proteins.

DNA-Directed RNA Polymerases↗
PubMed1988

Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins.

Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.

Amino Acid Sequence↗
PubMed1998

Cellular localization of a plant protein PSAM 1 in arbuscular mycorrhizas of Pisum sativum.

Psam 1 is a single-copy gene which is activated during early plant-fungal interaction in wild-type pea inoculated with Glomus mosseae and which codes for PSAM 1, a putative protein of 108 amino acids. A synthetic peptide was designed of 108 amino acids. A synthetic peptide was designed in an antigenic region of this protein to produce a polyclonal antibody against PSAM 1 and to investigate its cellular localization. Western blot analysis revealed that a polypeptide of about 14.5 kDa accumulated more in mycorrhizal than non-mycorrhizal pea roots. The PSAM 1 antigen was immunolocated in planta in arbuscule-containing cells of mycorrhizal roots and especially in the cytoplasm surrounding young arbuscules in cortical cells, which suggests that its accumulation is somehow related to the symbiotic state of these cells.

Animals↗
PubMed1999

Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A.

Proteins of approximately 35, 55 and 65kDa were purified from cauliflower extracts by microcystin-Sepharose chromatography and identified by amino acid sequencing as plant forms of protein (serine/threonine) phosphatase 1 (PP1) catalytic subunit, PP5 and a regulatory A-subunit of PP2A, respectively. Peptides that corresponded both to the tetratricopeptide (TPR) repeat and catalytic domains of PP5 were identified. Similar to mammalian PP5,the casein phosphatase activity of plant PP5 was activated >10-fold by arachidonic acid, with half-maximal stimulation occurring at approximately 100 microM lipid.

Amino Acid Sequence↗