Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cathepsin L was purified from carp hepatopancreas by a method involving ammonium sulfate precipitation and a series of column chromatographies, in which the enzyme had an affinity toward Concanavalin A and Cibacron Blue F3GA. Its homogeneity was established by Native-PAGE, but two protein bands corresponding to molecular masses of 30,000 (single chain) and 24,000 (heavy chain) migrated on SDS-PAGE. The enzyme exhibited a maximum activity for carbobenzoxy-L-phenylalanyl-L-arginyl-4-methylcoumaryl-7-amide (Z-Phe-Arg-MCA) at pH 5.5-6.0 and 50 degrees C and the remarkable stability at pH 5.0-6.5 and below 40 degrees C. All tested cysteine protease inhibitors and TLCK and chymostatin markedly inhibited its activity, whereas the other serine protease inhibitors and a metalloprotease inhibitor negligibly affected it. In addition, several metal compounds reduced either its activity or stability to differing extents. Although EDTA alone caused an only marginal activation of the enzyme, its maximum activation required both 2 mM cysteine and 1 mM EDTA. The enzyme had an ability to hydrolyze three peptidyl-MCA substrates including Z-Phe-Arg-MCA, but all kinetic constants indicate that Z-Phe-Arg-MCA is the optical substrate to the enzyme.
Comp Biochem Physiol B Biochem Mol Biol 1997 Nov
PMID:Purification and characterization of cathepsin L from hepatopancreas of carp Cyprinus carpio. 946 67

The open reading frame of a gene encoding a protein homologous to vertebrate fatty acid desaturases has been characterized in Drosophila melanogaster. This is the first description of a desaturase sequence in insects. Two cDNAs were cloned: the combined 1.5 kb nucleotide sequences indicate that the gene encodes a polypeptide of 383 amino acid residues with a high sequence similarity to the well defined delta 9 desaturases from rat and yeast and desaturases from carp and tick. The Drosophila protein contains two histidine cluster motifs (HXXHH) and two hydrophobic regions which are conserved among all desaturases, whereas the amino and carboxy ends look more variable. The desaturase gene seems to be expressed in adults at a low level, with a greater prevalence in females than in males. Two genomic sequences have been amplified by polymerase chain reaction (PCR), and have a very similar open reading frame but a different organization; one with three introns and the other without introns. Both seem to correspond to two distinct genes and have been named "desat locus". They are localized to a single locus, 87C, on the right arm of the third chromosome. The possible involvement of the desat product in the biosynthesis of D. melanogaster contact pheromones is discussed.
Insect Biochem Mol Biol 1997 Nov
PMID:Partial characterization of a fatty acid desaturase gene in Drosophila melanogaster. 950 19

The effect of phenoxyherbicides and their metabolites on the structure of oxy- and deoxyhemoglobin was studied by using different doses and times of incubation of hemoglobin with the herbicide. It was ascertained that among the investigated hemoglobins the most sensitive was carp oxyhemoglobin incubated with 2,4-D (2,4-dichlorophenoxyacetic acid) and the least sensitive was human hemoglobin. Comparing the toxicity of 2,4-D, MCPA (2-methyl-4-chlorophenoxyacetic acid), 2,4-DCP (2,4-dichlorophenol), 2,4-DMP (2,4-dimethylphenol) it was found that the highest decrease occurred in bovine hemoglobin incubated with 2,4-DMP. The phenoxyherbicides caused stabilization of the structure of T-deoxyhemoglobin in vitro, in that they decreased the oxygen affinity with a simultaneous increase in methemoglobin concentration.
Biochem Mol Biol Int 1998 Jun
PMID:Influence of phenoxyherbicides and their metabolites on the form of oxy- and deoxyhemoglobin of vertebrates. 963 29

Two chymotrypsins were purified from the hepatopancreas of grass carp (Ctenopharyngodon idellus) by chromatographies on phenyl-Sepharose and Q-Sepharose. The molecular weights of chymotrypsins I and II were 28 and 27 kDa, respectively. The two chymotrypsins showed similar susceptibility to inhibitions by phenylmethylsulfonyl fluoride and soybean trypsin inhibitor, but differed in their response to tosyl-L-phenylalanine chloromethyl ketone and aprotinin in which chymotrypsin I was more resistant. Chymotrypsin I was a less typical chymotrypsin and exhibited lower catalytic efficiency with the chymotrypsin-specific ester and amide substrates, when compared with chymotrypsin II. For both chymotrypsins, optimal activity was detected in the pH range 7.0-8.5.
Biochem Mol Biol Int 1998 Jun
PMID:Isolation of two chymotrypsins from grass carp. 967 63

The neurofilament (NF) polypeptides of the fish giant Mauthner cell axons (MAs) and their degree of phosphorylation were investigated in the adult by means of immunoblot and immunohistochemical staining. Fasciculus longitudinalis medialis (FLM) axons of much smaller caliber, among which MAs run in the ventral spinal cord, were also analyzed in two teleost fish belonging to continuously growing species. To detect NF polypeptide subunits, commercially available monoclonal antibodies against mammalian NF-L (68 kDa), NF-M (160 kDa), phosphorylated (P) and non-phosphorylated (nP) NF-H (200 kDa) epitopes were used. These antibodies labelled bands of the identical molecular weight in fish cervical spinal cord total protein immunoblots. A peculiar NF composition of the MAs was observed, following immunohistochemical staining i.e. a low NF-M expression and a codistribution of P and (nP)-NF-H epitopes. Moreover, on the basis of immunoperoxidase staining in ultrathin longitudinal MA sections, we suggest that P NF-H are arranged in bundles, whilst (nP)-NF-H are likely to be free in the axoplasm. By contrast, FLM axons were found reactive with antibodies only against P NF-H. These results confirm that in carp and trout, NF have epitopes cross-reacting with monoclonal antibodies directed against the mammalian NF subunits. Furthermore, as regards the co-distribution of phosphorylated and non-phosphorylated NF-H epitopes in the M-cell axons, these might be considered as not yet completely mature axons taking into account that carp and trout belong to continuously growing species.
Cell Mol Biol (Noisy-le-grand) 1998 Jun
PMID:Phosphorylated and non-phosphorylated neurofilament epitopes are co-distributed in the fish Mauthner axon. 967 96

We isolated a clone comprising four exons of the carp Pit-1 gene. Using synthetic oligonucleotide probes derived from the carp Pit-1 sequence Pit-1 expression was assessed by in situ hybridization in pituitary sections from summer- and winter-acclimatized carp. Semiquantitative analyses of the hybridization signals revealed a significant higher Pit-1 expression in the proximal pars distalis (PPD) and pars intermedia (PI) of the pituitary glands from summer-acclimatized carp, compared to the winter-acclimatized fish. In both adaptive states, relative to the PPD and PI, only a basal Pit-1 expression was detected in the rostral pars distalis. Thus, during seasonal acclimatization of an eurythermal fish, Pit-1 seems to be involved in the mechanisms that underlie the compensatory response.
Biochem Mol Biol Int 1998 Jul
PMID:Effect of seasonal acclimatization on the expression of the carp transcription factor Pit-1. 971 6

Expressed sequence tag (EST) analysis was adopted to address physiological changes after injection of carp pituitary extract for induction of ovulation. ESTs were analyzed from cDNA libraries constructed from mRNA isolated from channel catfish (Ictalurus punctatus) pituitaries before and after induction of ovulation by injection of carp pituitary extract. One hundred randomly picked clones were analyzed. Of the sequences generated, a large percentage (59%) of ESTs were identified as known genes by identity comparisons. These 59 clones of known gene products represent transcriptional products of 30 genes. The 41 clones of unknown gene products represent 33 genes. Expression of gonadotropin (GtH) alpha-subunit (149%) and prolactin (176%) was slightly enhanced as a result of induced ovulation. Large increases in frequencies of several peptide hormones were observed as a result of induced ovulation: GtH beta-I, 486%; GtH beta-II, 933%; growth hormone, 393%; proopiomelanocortin (POMC), 345%. POMC represented about 21% of all transcriptional activity in the pituitaries after induced ovulation. This is the first study addressing physiological changes after injection of carp pituitary extract, a procedure widely used in catfish hatcheries.
J Mol Endocrinol 1998 Oct
PMID:Transcriptional activities in the pituitaries of channel catfish before and after induced ovulation by injection of carp pituitary extract as revealed by expressed sequence tag analysis. 980 55

Proopiomelanocortin (POMC) is the precursor for a number of biologically active peptides such as adrenocorticotropic hormone (ACTH), alpha-melanocyte-stimulating hormone (alpha-MSH) and beta-endorphin. It is well known that these peptides are involved in the stress response in fish as well as in mammals. We have cloned two different carp POMC cDNAs called, POMC-I and POMC-II. The nucleotide sequences of 955 bp for POMC-I and 959 bp for POMC-II share 93.5% identity in their cDNAs, and the deduced amino acid sequences (both 222 amino acids) are 91.4% identical. In the ACTH and beta-MSH domain, two amino acid substitutions are found, whereas alpha-MSH and beta-endorphin are identical. For beta-MSH, the serine replacement (in POMC-I) by a glycine (in POMC-II) results in a putative amidation site Pro-X-Gly for POMC-II. We used RT-PCR to show that both POMC mRNAs are expressed in the hypophysis, hypothalamus and other parts of the brain of a single fish. Furthermore, in a phylogenetic tree based on POMC sequences the divergence of carp POMC-I and -II from tetraploid animals (salmon, trout and xenopus) is demonstrated.
Mol Cell Endocrinol 1998 Aug 25
PMID:Cloning and expression of two proopiomelanocortin mRNAs in the common carp (Cyprinus carpio L.). 980 47

An ovary-specific cystatin is immunocytochemically demonstrated to be localized in the chorions, cortical granules, and yolk granules of carp oocytes, as well as in the follicle cells surrounding oocytes. During cortical reaction, cystatin is exocytosed from cortical granules into the perivitelline space. In situ hybridization confirms that cystatin is synthesized by oocytes and follicle cells. Western blotting reveals that chorion cystatin appears in multiple bands of high molecular weight (from 65 kDa to larger than 200 kDa). No cystatin monomer of 14 kDa is found. These results indicate that chorion cystatin is conjugated with other chorion components. Two forms of conjugates are found. In one form, cystatin, ZP2, fibroin-like substance (FLS), and cathepsin-like substance (CLS) are conjugated, which is extracted by sodium dodecyl sulfate. In the other form, cystatin, FLS, and CLS are conjugated, which is extracted by guanidine thiocyanate (GTC). Most chorion cystatin of oocytes and ovulated eggs is solubilized by GTC, while a large amount of cystatin remains in the fertilization envelope of cortical reacted eggs after extraction by GTC.
Mol Reprod Dev 1998 Dec
PMID:Identification of cystatin as a component of carp chorion. 982 Feb 2

Goldfish pituitary contains two types of growth hormones. One with five cysteine residues (type-I) similar to other Cyprinid GHs, and the other with four Cys residues (type-II) similar to those of other fish and tertapod species. Recombinant goldfish type II GH (gfGH-II) was produced in Escherichia coli using the pRSETB expression vector. The gfGH-II was produced fused to a leader sequence, which sequestered into inclusion bodies after expression. The inclusion bodies were solubilized using sodium hydroxide and the fusion protein purified by chelating affinity chromatography. Subsequently, gfGH-II was cleaved and analyzed by Western blotting, using a specific antiserum. For comparison we also produced recombinant common carp GH (cGH) which has 95% similarity to gfGH-II, and tested their growth promoting activity in goldfish. Both forms of GH significantly increased the growth rate of goldfish (P < 0.05), although cGH was found to have a somewhat higher potency than gfGH-II.
Comp Biochem Physiol B Biochem Mol Biol 1998 Aug
PMID:Production of a biologically active novel goldfish growth hormone in Escherichia coli. 985 13


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