Purification and properties of alkaline ribonuclease from human serum

Akagi, Kenzo; Murai, Kenichi; Hirao, N.; Yamanaka, Masayoshi

doi:10.1016/0005-2787(76)90311-7

Cited by 62 publications

(56 citation statements)

References 17 publications

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“…All six dependences showed individual features of pH dependencies. In contrast to all SLE abzymes, RNases Lupus 58 have only one pH optimum (6.8-7.5) for hydrolysis of poly(A) [104][105][106] (Figure 8D). …”

Section: Polyclonal Dnase and Rnase Abzymesmentioning

confidence: 99%

“…The substrate specificity of SLE IgGs with RNase activity, however, was unique within certain limits for Abs from every individual SLE patient [11]. In contrast to human RNases, SLE IgGs effectively hydrolyze the most resistant poly(A) substrate for all known human RNases [104][105][106][107][108][109]. SLE IgGs demonstrated a very slow hydrolysis of poly(C) [11], which is the best substrate for all mammalian RNases [104][105][106].…”

Section: Polyclonal Dnase and Rnase Abzymesmentioning

confidence: 99%

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Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Nevinsky¹

2017

Lupus

321

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Systemic lupus erythematosus (SLE) is known as a systemic polyethiologic diffuse autoimmune disease characterized by connective tissue disorganization and the paramount damage of skin and visceral capillaries. Usually, SLE symptoms include high fever, hair loss, mouth ulcers, chest pain, swollen lymph nodes, painful and swollen joints, increased fatigue, and appearance of red rash more often on the face. The exact reason of SLE appearance is not really clear. Detection of catalytic Abs (abzymes) was shown to be the earliest indicator of different AI disease development. Some abzymes are cytotoxic and can play a dangerous negative role in the pathogenesis of AI diseases. SLE is characterized by the appearance of abzymes with several different catalytic functions including hydrolysis of peptides and proteins, DNA, RNA, and oligosaccharides. In addition, monoclonal SLE abzymes are characterized by extraordinary diversity in the affinity to the substrates, physicochemical and catalytic characteristics, optimal conditions of catalysis, cytotoxicity, etc. Production of abzymes in SLE mice is associated with changes in the differentiation of hematopoietic stem cells of bone marrow, increase in lymphocyte proliferation, and significant suppression of cell apoptosis in different organs. In this chapter, abzymes with different catalytic activities in SLE are described.

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Section: Polyclonal Dnase and Rnase Abzymesmentioning

confidence: 99%

Section: Polyclonal Dnase and Rnase Abzymesmentioning

confidence: 99%

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Nevinsky¹

2017

Lupus

321

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“…It has been reported that the inhibitory effects of poly(A) on the spleen RNase were reversed to a considerable extent by the polyamine, spermidine [Ill, and that the effects of polyamines on human serum RNase were due to their appar- ent ability to control the degree of aggregation of the enzyme [22]. Hemin is also known to inhibit reticulocyte RNase, which may be a type of nonsecretory RNase, but does not inhibit pancreatic RNase [23].…”

Section: Cu Taly Tic Pvopert Iesmentioning

confidence: 99%

Purification and characterization of a ribonuclease from human spleen

Yasuda

Mizuta

Sato

et al. 1990

European Journal of Biochemistry

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A ribonuclease has been isolated from human spleen (RNase HS) by means of acid extraction, ammonium sulphate fractionation, successive column chromatographies on CM-cellulose, heparin-actigel, and poly(G)-agarose, and double gel-filtration on Sephadex G-75. The purified preparation was homogeneous as judged by SDSIPAGE. RNase HS was found to be a glycoprotein, containing three fucose, one mannose and five glucosamine residues/molecule, with a molecular mass of 17 kDa as determined by both SDS/PAGE and gel filtration. The catalytic properties and structural features, including its amino acid composition and the amino acid sequence of the N-terminal 35 residues, indicated that the enzyme was strictly related to nonsecretory RNase isolated from human urine and liver. In particular, the amino acid sequence of the N-terminal was identical with that of urine nonsecretory RNase and eosinophil-derived neurotoxin. Furthermore, analyses using three different antibodies specific to RNase HS, urine nonsecretory RNase and urine secretory RNase, indicated that RNase HS was not immunologically distinguishable from urine nonsecretory RNase, but clearly so from urine secretory RNase. However, the carbohydrate compositions of RNase HS and urine nonsecretory RNase were found to differ. It therefore remains to be resolved whether or not the tissue of origin of nonsecretory RNase in urine is the spleen.Sierakowska and Shugar [ 11 classified the pyrimidinespecific neutral and alkaline ribonuclease (RNase) of mammalian origin into two distinct classes : secretory and nonsecretory RNases. The former enzyme shows a pH optimum of around 8.5 and a greater preference for poly(C) than poly(U) and RNA. The latter cleaves RNA most effectively at pH 7.0, and its preference for poly(C) is less than the former.

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“…Alanine aminotransferase [18], acetylesterase [19], acid DNase [20], inosine diphosphatase [21], galactosyl transferase [22,23], acid phosphatase [24,25], acid phosphodiesterase [26,27], acid proteinase [14], amannosidase [25], a-glucosidase [27,28] and acid RNase [29] were measured essentially by published methods. To minimize the contribution of acid phosphatase activity, the assay mixture for acid phosphodiesterase was supplemented with 20 mM glycerol-2-phosphate.…”

Section: Parasitesmentioning

confidence: 99%

Subcellular Fractionation of Trypanosoma brucei Bloodstream Forms with Special Reference to Hydrolases

1980

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Bloodstream forms of Trypanosoma brucei have been screened for the presence of enzymes that could serve as markers for the plasma membrane, flagellar pocket, lysosomes, endoplasmic reticulum and Golgi apparatus in order to study the subcellular organization of the digestive system of the parasite.Acetylesterase, acid DNase, acid phosphatase, acid phosphodiesterase, acid proteinase, acid RNase, alanine aminotransferase, galactosyl transferase, a-glucosidase, inosine diphosphatase and a-mannosidase were partially characterized and their assays optimized for pH-dependent activity, linearity of reaction with respect to incubation time and enzyme concentration, and the effect of inhibitors and activators. The association of these enzymes with particulate material and the presence of structural latency were investigated.Acid proteinase and a-mannosidase are particle-bound and latent in cytoplasmic extracts ; they can be activated and solubilized in part by Triton X-100. Similar results were obtained for acid phosphatase, acid phosphodiesterase and inosine diphosphatase. Neutral a-glucosidase, though partly sedimentable, does not show latency and is readily solubilized by the detergent. Galactosyl transferase is firmly membrane-bound even in the presence of 0.1 % Triton X-100, Cell fractionation by differential centrifugation and density equilibration on sucrose gradients revealed that both a-mannosidase and acid proteinase are associated with organelles that band at a density of about 1.20 g/cm3. Inosine diphosphatase, galactosyl transferase, acid phosphatase and acid phosphodiesterase sediment predominantly as microsomal constituents equilibrating at densities between 1.13 and 1.15 g/cm3. In addition, inosine diphosphatase and galactosyl transferase exhibit considerable activity at higher densities (1.18 -1.25 g/cm3). Neutral a-glucosidase is mainly recovered in the nuclear and microsomal fraction; its particulate part equilibrates as a single band at e = 1.22 g/cm3. Acetylesterase and acid DNase are largely soluble, whereas acid RNase does not produce distinct sedimentation and banding profiles.In intact cells, neutral a-glucosidase and acid phosphatase appear to be highly accessible to their substrates.It is tentatively concluded that (a) acid proteinase and a-mannosidase are lysosomal enzymes, (b) acid phosphatase and acid phosphodiesterase are associated with the flagellar pocket and part of the former enzyme probably with the endoplasmic reticulum, (c) galactosyl transferase is a constituent of the Golgi apparatus, and (d) a-glucosidase may serve as a marker for the plasma membrane. Inosine diphosphatase may also be derived from the latter structure.

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Purification and properties of alkaline ribonuclease from human serum

Cited by 62 publications

References 17 publications

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Catalytic Antibodies in Norm and Systemic Lupus Erythematosus

Purification and characterization of a ribonuclease from human spleen

Subcellular Fractionation of Trypanosoma brucei Bloodstream Forms with Special Reference to Hydrolases

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