Further characterization of human eosinophil peroxidase

Olsen, R L; Syse, K; Little, C. H. A.; Christensen, Terje

doi:10.1042/bj2290779

Cited by 16 publications

(10 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It appears that eosinophil peroxidase has more than one antigenic determinant of which one is similar to the gastric peroxidase and another is similar to the intestinal enzyme. Intestinal peroxidase has been suggested to contain carbohydrate [3] and human eosinophil peroxidase has been shown to include carbohydrate [36]. However, negative periodic acid/Schiff staining in both native and denatured gastric peroxidase indicates that it does not contain carbohydrate.…”

Section: Discussionmentioning

confidence: 99%

Purification, characterization and origin of rat gastric peroxidase

Banerjee

1986

European Journal of Biochemistry

View full text Add to dashboard Cite

A membrane-bound peroxidase (EC 1.1 1.1.7) from rat stomach has been solubilized by 0.2% cetyltrimethylammonium bromide in the presence of 1.2 M NH4Cl. The enzyme was purified 3355-fold to apparent homogeneity as judged by acid polyacrylamide gel electrophoresis and appears to be a cationic protein. In sodium dodecyl sulfate gel electrophoresis, the enzyme shows single polypeptide band of M , 45000. In gel permeation, the M , has been estimated as 47000. Spectral properties indicate the presence of Soret band at 412 nm which shifts to 425 nm on complexation with CN-and to 430 nm on reduction with dithionite. The velocity constant, kl for the reaction of the proxidase with H202 is 1.38 x lo7 M-' s-' and K,,, for H,O, is 0.1 mM. The enzyme contains active sulphydryl groups and is inhibited by sulphydryl reagents of which p-hydroxymercuribenzoate is more reactive than mersalyl or N-ethylmaleimide. The enzyme is very resistant to thermal denaturation up to 65°C and also to chaotropic reagents at least up to 2 M above which it is inactivated. The enzyme shows similarity with the intestinal eosinophil peroxidase as regards the molecular mass, spectral, kinetic and some of the catalytic properties. However, they differ significantly in terms of their interaction with fluoride ion, sulphydryl reagents, chaotropic reagent and also with the antiserum against the gastric peroxidase. Histochemically, the gastric peroxidase is shown to be localised in the gastric gland proper of the fundic stomach, rich in parietal and chief cells.After the suggestion of Rytomaa and Teir tha't all animal tissue peroxidases (except thyroid and myeloperoxidase) are contributed by the eosinophils [l], the properties of the peroxidases purified from various tissues have been compared [2 -161 in order to establish whether the enzyme is distinct and intrinsic to each tissue or it is derived from the contaminating eosinophils. Recently King et al. [17] and Olsen and Little [5] have shown that estrogen-induced peroxidase in rat uterus is mainly contributed by the eosinophils. The enzyme from pig and rat intestine has also been characterized and shown to have some similarities with eosinophil peroxidase [2, 31. Very recently we have established that rat intestinal peroxidase is not an endogenous enzyme and is mainly derived from the eosinophils accumulating in the core of the intestinal villi [18].The presence of a highly active peroxidase in mouse gastric mucosa and its cellular and subcellular localization was reported earlier from our labortory [19]. Recently we have shown that this enzyme in rat gastric mucosa is modulated by adrenal glucocorticoids [20]. However, it is not established yet whether gastric peroxidase is an enzyme intrinsic to the tissue or is contributed by the eosinophls, as in the case of intestinal peroxidase [18]. We have isolated homogeneous gastric peroxidase and its molecular, spectral, kinetic, catalytic and immunological properties have been studied and compared with those of the intestinal eosinophil peroxidase. The data...

show abstract

Section: Discussionmentioning

confidence: 99%

Purification, characterization and origin of rat gastric peroxidase

Banerjee

1986

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Even though there is evidence for the use of truncated tRNA primers (36)(37)(38) or incorrectly processed tRNA (39), the insertion of 2 bases completely eliminated the PBS function in reverse transcription. Because of the homology, tRNA anneals efficiently to the genomic RNA PBS and is able to initiate the reverse transcription process in the wild type (Fig.…”

Section: Methodsmentioning

confidence: 99%

Mutation in the primer binding site of the type 1 human immunodeficiency virus genome affects virus production and infectivity.

Nagashunmugam

Ayyavoo

Goldsmith

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

In an effort to understand the contribution of the primer-binding site (PBS) region to human immunodeficiency virus (HIV) replication, we have constructed a mutant HIV proviral DNA with an alteration in the 5' end of the PBS. The PBS mutant proviral DNA was characterized by transfection of the viral DNA into CD4' and non-CD4' target cells.The results indicate that mutation in the PBS reduced the level of viral particles released into the medium of transfected cells in comparison to wild-type proviral DNA. The viral particles were noninfectious upon transmission to established CD4' cell lines and phytohemagglutinin-stimulated peripheral blood lymphocytes. Electron microscopic analysis of the transfected cells revealed no abnormalities in the structure of the virion directed by the mutant proviral DNA. Also, the protein and RNA contents of the mutant virions were similar to the wild type. The quantitation of intracellular viral structural protein in the transfected cells, however, indicated that the PBS mutation may have an effect on the assembly of viral particles in addition to completely abolishing reverse transcription of viral RNA into DNA. These results provide evidence that the PBS region of the viral genome has multiple functions in HIV-I replication.

show abstract

“…2 and 4), we estimate that 1 out of every 10-20 viruses could mutate by this mechanism during a single cycle of replication. Studies of unintegrated proviral DNAs from infected cells in culture suggest that blunt-end addition occurs widely in retroviruses (24)(25)(26)(27)(28) and in the retroelement copia (29), although the frequency in vivo appears somewhat lower than in vitro (27,28,30,31).…”

Section: Biochemistry: Patel and Preston 552mentioning

confidence: 99%

Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends.

Patel

Preston

1994

Proc. Natl. Acad. Sci. U.S.A.

141

100

View full text Add to dashboard Cite

Human immunodeficiency virus type 1 (HIV-1) is genetically highly variable. This is attributed to the error-prone nature of HIV-1 replication and its proclvity for recombination. During replication and recombination, reverse transcriptase (RT) must polymerize DNA to the 5' ends of multiple RNA and DNA template termini while converting HIV-1 RNA to double-stranded DNA. We have determined the fidelity of HIV-1 RT in vitro during polymerization to the 5' ends of HIV-1 long terminal repeat DNA template sequences and to the end of a partial HIV-1 genomic RNA template that mimics a recombination intermediate. HIV-1 RT readily extended recessed DNA primers to form full-length blunt-end DNA-DNA and DNA-RNA duplexes. In addition, HIV-1 RT catalyzed high yields of products with one to four extra nucleotides at the 3' ends of the nascent DNAs. These products were formed processively via a nontemplated mechanism that is highly specific for the addition of purine nucleotides (A > G >> T . C). Thus, HIV-1 RT is extremely unfaithful at both DNA and RNA template ends, introducing errors (extra nucleotides) in one out of every two or three nascent strands processively polymerized. This error rate is 1000 times higher than for HIV-1 RT-catalyzed errors at internal template positions. Blunt-end additions were also catalyzed by other retroviral RTs at relative rates of HIV-1 Moloney murine leukemia virus > avian myeloblastosis virus. These data suggest a potentially important mechanism for retroviral mutation mediated by nontemplated blunt-end addition of purines prior to forced copy-choice recombination.

show abstract

Further characterization of human eosinophil peroxidase

Cited by 16 publications

References 31 publications

Purification, characterization and origin of rat gastric peroxidase

Purification, characterization and origin of rat gastric peroxidase

Mutation in the primer binding site of the type 1 human immunodeficiency virus genome affects virus production and infectivity.

Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends.

Contact Info

Product

Resources

About