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PubMed1994

Molecular cloning and characterization of the full-length cDNA encoding the developmentally regulated lysosomal enzyme beta-glucosidase in Dictyostelium discoideum.

The developmentally regulated Dictyostelium discoideum lysosomal enzyme beta-glucosidase is synthesized as a membrane-associated glycosylated precursor polypeptide which undergoes at least two proteolytic cleavage events to generate a soluble mature lysosomally localized protein. To begin to analyze the mechanisms regulating the sorting of this protein and the regulation during development of the expression of the encoding gene, we have cloned and sequenced a 2.6-kilobase (kb) cDNA which contains a complete 2463-nucleotide open reading frame coding for beta-glucosidase. Conceptual translation of this open reading frame predicts a polypeptide similar in molecular mass to the primary translation product of 94 kDa that also contains the same amino acid sequences of two V8 protease derived-peptides generated from the purified beta-glucosidase enzyme. The D. discoideum enzyme contained regions highly homologous at the amino acid sequence level to both bacterial and fungal beta-glucosidases, although these regions did not overlap. A potential cleavable signal sequence was also found in the first 21 amino acids followed by a highly polar stretch of 49 amino acids which (based on amino acid sequencing of the mature beta-glucosidase) represents a pro region for this protein. This region is similar in location, size, and charge to the D. discoideum alpha-mannosidase pro-I region (Schatzle, J., Bush, J., and Cardelli, J. (1992) J. Biol. Chem. 267, 4000-4007). Several small hydrophobic stretches of amino acids were also distributed throughout the protein; however, no obvious transmembrane region(s) were identified which might explain the observed membrane association of the precursor protein. Finally, Northern blot analysis indicated that the gene encoding this enzyme was under developmental regulation. The steady state level of a 2.7-kb beta-glucosidase mRNA decreased significantly during the aggregation stage of development, from high levels during growth, and then increased in the form of a larger size 2.8-kb mRNA during the final stages of development.

Age Factors↗
PubMed1984

Studies on the mechanism of castanospermine inhibition of alpha- and beta-glucosidases.

Castanospermine (1,6,7,8-tetrahydroxyoctahydroindolizine) is an indolizidine alkaloid that was isolated from the Australian plant, Castanospermum australe. This alkaloid was found to be a potent inhibitor of lysosomal alpha- and beta-glucosidases. In this report, the mechanism of inhibition of amyloglucosidase (an exo-1,4-alpha-glucosidase) and almond emulsin beta-glucosidase was examined. Castanospermine proved to be a competitive inhibitor of amyloglucosidase at both pH 4.5 and 6.0 when assayed with the p-nitrophenyl-alpha-D-glucoside. It was also a competitive inhibitor of almond emulsin beta-glucosidase at pH 6.5, but in this case previous studies had shown that inhibition was of the mixed type at pH 4.5 to 5.0. Th pH of the incubation mixture had a marked effect on the inhibition. Thus, in all cases, castanospermine was a much better inhibitor at pH 6.0 to 6.5 than it was at lower pH values. The pK for castanospermine was found to be 6.09, indicating that the alkaloid was probably more active in the unprotonated form. This was also suggested by the fact that the N-oxide of castanospermine, while still a competitive inhibitor, was 50 to 100 times less active than was castanospermine, and its activity was not markedly altered by pH. These results probably explain why castanospermine is a good inhibitor of the glycoprotein processing enzyme, glucosidase I, since this is a neutral enzyme.

Alkaloids↗
PubMed1983

Beta-glucosidase excretion in Trichoderma strains with different cell wall bound beta-1,3-glucanase activities.

Two different strains of Trichoderma pseudokoningii (SE1 A8 and SE1 D81) and Trichoderma viride QM 9123 release into the medium different proportions of the total beta-glucosidase activity produced. This observation correlates with the degree of beta-1,3-glucanase binding to the cell wall found for each strain. DEAE-Sephadex ion-exchange chromatography revealed three peaks of beta-1,3-glucanase activity. These three enzymes (enzyme I, enzyme II, and enzyme III) differ in their extent of binding to the cell walls, their activity on isolated cell walls and Trichoderma beta-glucan, and their affinity for beta-glucan. Of these enzymes, enzyme II shows the largest variation in relative importance among the three strains and is located predominantly within the mural compartment. Enzyme II has the highest activity on and affinity for Trichoderma beta-glucan. Enzyme II is also the most active in releasing beta-glucosidase from cell walls of strain SE1 A8 (the strain excreting a high proportion of its beta-glucosidase into the culture fluid) as well as from strain SE1 D81 (little beta-glucosidase activity in the culture fluid). It is concluded that the action of beta-1,3-glucanase II on cell wall beta-glucan may be responsible for the in vivo release of cell wall bound beta-glucosidase into the culture fluid.

Cell Wall↗
PubMed1979

Neutral alpha-glucosidase from human kidney. Molecular and immunological properties. Relationship with intestinal glucoamylase.

Some molecular properties of the purified neutral alpha-glucosidase from human kidney were studied. The enzyme is a glycoprotein with high molecular weight (315000-352000 according to the method used). Its sedimentation coefficient is 12.9S. It exhibits at least three peaks of activity in isoelectric focusing experiments. This heterogeneity appears to be related to sialic acid residues from the carbohydrate moiety. An anti-human renal alpha-glucosidase antiserum was raised from rabbit. The antiserum effect on human intestinal maltases was studied in immunodiffusion experiments. An identity pattern was observed between renal neutral alpha-glucosidase and intestinal glucoamylase. No precipitation occurred with intestinal sucrase. Renal neutral alpha-glucosidase and intestinal glucoamylase were both completely precipitated by the antiserum, their maltase activity being only slightly inhibited in the antigen-antibody complex. From their molecular and immunological properties a large homology appears between human renal alpha-glucosidase and intestinal glycoamylase.

Glucan 1,4-alpha-Glucosidase↗
PubMed1999

Intracellular transport of acid beta-glucosidase and lysosome-associated membrane proteins is affected in Gaucher's disease (G202R mutation).

Gaucher's disease (GD) is caused by an inherited deficiency of acid beta-glucosidase with storage of glucosylceramides in the lysosomes of macrophages. This study identifies a G202R mutation in the acid beta-glucosidase gene in an infant with severe neuronopathic (type 2) GD and only slightly reduced acid beta-glucosidase activity. Western blot analysis, pulse chase experiments, and the thin frozen section immunogold method were used to analyse the implications of this mutation on the pathogenesis, clinical heterogeneity and diagnostic evaluation of GD. The results show that acid beta-glucosidase persists in the patient's fibroblasts as a mannose-rich polypeptide in the endoplasmic reticulum and is not transported to the lysosomes. By contrast, high expression of the lysosome-associated membrane proteins LAMP-1 and LAMP-2, saposin C, and cathepsin D was observed in the patient's lysosomes. Immunogold labelling of the integral membrane proteins LAMP-1 and LAMP-2 increases significantly at the cell surface of Kupffer cells and fibroblasts as well as at the apical membrane of hepatocytes. In addition, LAMP-1 and LAMP-2 associate with the bilayer of stored glucosylceramide. It is concluded that defective intracellular transport of mutant acid beta-glucosidase from the endoplasmic reticulum to lysosomes leads to a more severe clinical phenotype than the residual enzyme activity may indicate. Furthermore, the detection of LAMP in the tubular bundles of undigested glucosylceramides, as well as their increased concentration at the surfaces of the affected cells, suggests that these proteins play a role in the storage or removal of substrate in GD. Intracellular targeting of acid beta-glucosidase and LAMP contributes to the broad phenotypic heterogeneity of GD.

Antigens, CD↗
PubMed1988

Effects of graded alpha-glucosidase inhibition on sugar absorption in vivo.

The effect of inhibition of disaccharidases on the degree of absorption of glucose, lactose, and sucrose was examined utilizing an in vivo model in the rat. Acarbose, a competitive alpha-glucosidase inhibitor was utilized to selectively inhibit small intestinal mucosal enzymes. Adult rats (250-350 g body weight) were the subjects of intraduodenal bolus infusion experiments with either sugar alone or sugar plus acarbose. All sugars were infused at a dose of 0.5 g/kg body weight. Portal venous blood glucose was determined at 30-min intervals from 0 to 150 min. Glucose (monosaccharide) and lactose (beta-galactoside) absorption were not altered by the presence of acarbose. In contrast, sucrose (alpha-glucosidase) absorption was significantly diminished in the presence of acarbose. Sucrose absorption in the presence of increasing acarbose doses (0.7-5.6 mg/kg body weight) was depressed in a dose-dependent fashion. Linear regression analysis revealed a high degree of correlation between residual sucrase activity and area under blood glucose curve (r = 0.9837). Similar degrees of correlation were found between acarbose dose and area under blood glucose curve (r = -0.9322), and between residual sucrase activity and acarbose dose (r = -0.9695). These data confirm that acarbose is a selective alpha-glucosidase inhibitor that does not affect monosaccharidase transport. In the presence of acarbose, alpha-glucosidase absorption is diminished in a dose-dependent fashion. Postprandial glucose rise following an alpha-glucosidase meal seems to be determined, in the presence of graded acarbose inhibition, by residual mucosal alpha-glucosidase activity.

Acarbose↗
PubMed2004

Analysis of gene expression in yeast protoplasts using DNA microarrays and their application for efficient production of invertase and alpha-glucosidase.

The global gene expression of cultured Saccharomyces cerevisiae protoplasts was compared with that of cells using DNA microarray. Quantitative and qualitative analyses revealed that after 6 h of cultivation, 416 gene transcript levels (about 7.1% in all) in the cultured protoplasts were different from those in the cells. Various characteristics and functions of the protoplasts were predicted from the analysis of the gene functions. The cultured protoplasts were more sensitive to oxidative stress than the cultured cells. Their cell cycles were arrested at the G1 phase and cell wall synthesis was promoted. Carbohydrate metabolism was activated in cultured protoplasts, while amino acid biosynthesis was inhibited. Furthermore, some genes associated with the secretory pathway of metabolites were activated, leading to active secretion of these metabolites into the broth. As an example of the application of DNA microarray analysis, we developed two novel methods for the production of useful enzymes based on the characteristics of protoplasts. One was the production of invertase based on the activated secretory pathway, while the other was the production of alpha-glucosidase based on the activated carbohydrate metabolism. The secretion of invertase and alpha-glucosidase was promoted in cultured protoplasts. The invertase and alpha-glucosidase productivities in the cultured protoplasts were 657 U and 218 U, respectively. On the other hand, only 227 U of invertase was produced, while alpha-glucosidase was not detected, in the cultured cells. The fragile protoplasts were immobilized in agarose gel to protect them from hydrodynamic stress. Four repeated-batch cultures with the immobilized protoplasts were performed, leading to the production of 1574 U of invertase and 739 U of alpha-glucosidase. The same productivities were obtained when this system was scaled up by 10-fold (invertase: 13304 U; alpha-glucosidase: 7688 U).

Journal Article↗
PubMed2006

Antiviral effect of alpha-glucosidase inhibitors on viral morphogenesis and binding properties of hepatitis C virus-like particles.

Hepatitis C virus (HCV) infections are a major public-health concern. New antiviral drugs are needed urgently to complement and improve the efficacy of current chemotherapies. The morphogenesis of HCV represents an interesting, and still unexploited, novel molecular target. alpha-Glucosidase inhibitors derived from the glucose analogue deoxynojirimycin (DNJ) inhibit viral morphogenesis in cellulo via perturbation of the N-glycosylation pathway and hence the misfolding of viral glycoproteins that depend on certain N-glycans for correct folding. Due to the heavy N-glycosylation of HCV glycoproteins, it was hypothesized that such inhibitors would also affect HCV morphogenesis. To study the effect of alpha-glucosidase inhibitors on viral morphogenesis and binding properties, HCV virus-like particles (VLPs) were produced by using baculovirus loaded with HCV structural-protein genes. Here, it is demonstrated that, in the presence of these alpha-glucosidase inhibitors, viral glycoproteins synthesized and retained in the endoplasmic reticulum (i) contain unprocessed, triglucosylated N-glycans, (ii) are impaired in their interaction with calnexin and (iii) are at least partially misfolded. Moreover, it is shown that, although the production of VLPs is not affected by alpha-glucosidase inhibitors, these VLPs contain unprocessed, triglucosylated N-glycans and potentially misfolded glycoproteins. Finally, it is demonstrated that VLPs produced in the presence of alpha-glucosidase inhibitors have impaired binding properties to hepatoma cells. The inhibitors of morphogenesis studied here target steps of the HCV viral cycle that may prevent or delay viral resistance. These alpha-glucosidase inhibitors may prove to be useful molecules to fight HCV infection in combination protocols.

Animals↗
PubMed2006

alpha-Glucosidase inhibitors have a prolonged antiviral effect against hepatitis B virus through the sustained inhibition of the large and middle envelope glycoproteins.

Previous work has shown that the secretion of enveloped hepatitis B virus (HBV) DNA and the HBV middle envelope protein (MHBs) are sensitive to glucosidase inhibition. Here, it is shown that HBV DNA secretion remains depressed after the removal of the glucosidase inhibitor and long after glucosidase function returns to normal. For example, glyco-processing and the secretion of alpha-1 anti-trypsin returned to normal within 3 h of the removal of the glucosidase inhibitor. In contrast, the secretion of HBV did not return to normal for more than 7 days after the removal of the inhibitor. Consistent with the inhibition of HBV virion secretion, the levels of HBV L and HBV M proteins were also reduced by treatment with the glucosidase inhibitor and remained reduced for 7 days after compound withdrawal. The implications of the prolonged antiviral effect against HBV and the use of glucosidase inhibitors as antiviral agents are discussed.

1-Deoxynojirimycin↗
PubMed1997

Enzyme therapy in Gaucher disease type 1: effect of neutralizing antibodies to acid beta-glucosidase.

Gaucher disease type 1, a non-neuronopathic lysosomal storage disease, is caused by mutations at the acid beta-glucosidase locus. Periodic infusions of macrophage-targeted acid beta-glucosidase reverse hepatosplenomegaly, hematologic, and bony findings in many patients. Two patients receiving enzyme therapy developed neutralizing antibodies to acid beta-glucosidase that were associated with a lack of improvement or progressive disease. After initial improvement, case 1 had no additional response to 2 years of high-dose (50 U/kg every 2 weeks) enzyme therapy. Similarly, case 2 initially showed a favorable response to enzyme therapy that plateaued after 1 year of treatment. Both patients developed minor allergic reactions and antibodies to acid beta-glucosidase within the first 6 months of treatment. Enzyme therapy was discontinued in case 1, with resultant disease progression and need for splenectomy. An immunosuppression/tolerization protocol was initiated in case 2 because of disease progression and stable neutralizing antibody titers. The IgG neutralizing antibodies rapidly and completely inactivated the wild-type, but not the N370S, acid beta-glucosidase in vitro. Antibodies to human serum albumin and chorionic gonadotropin also developed. The finding of neutralizing antibodies to acid beta-glucosidase during enzyme therapy for Gaucher disease has significant implications for monitoring the therapeutic responses and for potential alternative future therapies for Gaucher disease.

Adolescent↗
PubMed1982

Evidence for the deficiency of beta-glucosidase-activating factor in fibroblasts of patients with I-cell disease.

Reduced activity of beta-glucosidase was shown in the cultured skin fibroblasts of four patients with I-cell disease when the enzyme was tested without the use of detergents. In the presence of taurocholate and triton X100 beta-glucosidase activity was normal. This suggested a deficiency of a beta-glucosidase activating factor in I-cell fibroblasts rather than of the enzyme itself. The deficiency of beta-glucosidase activity was corrected to some extent by mixing cell lysates, and more effectively by cocultivation and fusion of I-cell disease and Gaucher fibroblasts. These results present evidence for the presence of a beta-glucosidase-activating factor in normal and Gaucher fibroblasts. In fibroblasts of patients with I-cell disease this activator is probably deficient, as is the case for most lysosomal enzymes.

Cells, Cultured↗
PubMed1984

Cloning and expression of the structural gene for beta-glucosidase of Kluyveromyces fragilis in Escherichia coli and Saccharomyces cerevisiae.

Cellobiose, the last product in cellulose degradation, is converted into two molecules of glucose by a beta-glucosidase. S. cerevisiae does posses the structural gene for a beta-glucosidase, but it is very poorly expressed; we thus decided to isolate and characterize that of Kluyveromyces fragilis. We constructed in E. coli HB101 strain a genomic library of the Kluyveromyces fragilis Y610 strain (ATCC 12424), a yeast able to grow on cellobiose and which constitutively produces the beta-glucosidase. The structural gene for beta-glucosidase was identified by its expression in E. coli. The initial isolated cosmid KF1 contained an insert of 35 Kb and by successive subcloning the insert size was reduced to 3.5 Kb (KF4). This cloned beta-glucosidase gene introduced in S. cerevisiae by transformation is expressed at a level of about 500 times that of K. fragilis. We checked by Southern hybridization that the high expression level was not due to a rearrangement of K. fragilis DNA during the cloning experiments. Nevertheless to obtain yeast transformants able to grow on cellobiose a yeast strain whose permeability to sugar is increased must be used and this last point is discussed.

Ascomycota↗
PubMed1979

Studies on the possible identity of particulate beta-glucosidase and beta-xylosidase of mouse liver.

Mouse liver beta-glucosidase (beta-D-glucosidase glucohydrolase, EC 3.2.1.21) and beta-xylosidase (1,4-beta-D-xylan xylohydrolase, EC 3.2.1.37) activities were studied under different conditions of incubation in an attempt to determine whether these two activities are due to a single enzyme or two separate enzymes. The results showed that: (a) Particle-bound beta-glucosidase and beta-xylosidase activities exhibit similar characteristics with different buffers and at various pH values, in the presence or absence of taurocholate. (b) Both activities are inhibited by gluconolactone and conduritol B eposice. beta-Glucosidase activity is inhibited competitively by the two inhibitors, but beta-xylosidase activity is inhibited non-competitively. (c) Xylonolactone was a very poor inhibitor of both activities, but the inhibition of beta-xylosidase activity was more pronounced than that of beta-glucosidase. (d) The presence of glucosides or xylosides simultaneously in the incubation medium suggested the presence of one enzyme with both activities. These results, together with the mode of inhibition produced by gluconolactone and conduritol B epoxide also suggest the presence of two different binding sites for the beta-D-glucoside and beta-D-xyloside, respectively.

Animals↗
PubMed1989

Beta-glucosidase activity in porcine epidermis.

One of the final steps in epidermal differentiation is the conversion of glucosylceramides to ceramides, which presumably is mediated by a beta-glucosidase activity. In the present manuscript, it is demonstrated that pig epidermis contains beta-glucosidase activity which is 3.3-times greater than alpha-glucosidase and 5-times greater than beta-galactosidase. This beta-glucosidase was found to be maximally active between pH 3.0 and essentially inactive at pH 9.0. In a standard assay, a disk of epidermis (8 mg dry weight) was submerged in 1 ml of 50 mM acetate buffer (pH 4.7) containing 150 mM NaCl and 15 mM p-nitrophenyl-beta-D-glucopyranoside at room temperature. Reaction was stopped by addition of 4 ml of 100 mM (pH 9.0) borate buffer and the supernatant was transferred to a separate tube. The nitrophenylate anion was then measured spectrophotometrically at a wavelength of 405 nm. Under these conditions, product formation was linear for at least 90 min and an apparent Km of 244 microM was estimated for the synthetic substrate. When the amount of epidermis in the assay was varied, the formation of product per unit of time remained proportional to the amount of epidermis. The level of beta-glucosidase activity was enhanced slightly by the inclusion of sodium taurocholate.

Animals↗
PubMed1978

Separation of acid and neutral alpha-glucosidase isoenzymes from fetal and adult tissues, cultivated fibroblasts and amniotic fluid cells by DEAE-cellulose and sephadex G-100 column chromatography.

Isoenzymes of alpha-glucosidases (EC 3.2.1.20) from various human organs and body fluids from fetuses and adults were separated by DEAE-cellulose column chromatography and gel filtration using Sephadex G-100. A minicolumn (0.35 X 2.5 cm) was used for the DEAE-cellulose column chromatography of extracts from tissues as well as cultivated cells of skin fibroblasts and amniotic fluid. The enzyme activity in the eluates was measured by the use of a methylumbelliferyl derivative as substrate and a very sensitive Microscope fluorimeter. In most tissue samples alpha-glucosidase was eluted mainly as a single peak when monitored at acid pH and as two peaks when the activity was measured at neutral pH in both columns. Another small peak representing alpha-glucosidase was found in fresh extracts of cultured cells on DEAE-cellulose columns. Neutral alpha-glucosidase especially in fibroblasts was extremely sensitive to storage at -20 degrees C. DEAE-cellulose column chromatography of plasma and amniotic fluid showed similar elution patterns of alpha-glucosidase. Differences were noticed in the elution pattern of urine from infants and adults. The tissue distribution and the different characteristics of the enzyme in samples of various origins and ages were discussed.

Adult↗
PubMed1980

Assay of the beta-glucosidase activity with natural labelled and artificial substrates in leukocytes from homozygotes and heterozygotes with the Norrbottnian type (Type 3) of Gaucher disease.

Leukocytes were isolated from 14 patients (7 males and 7 females ) with Gaucher disease of the Norrbottnian type (Type 3), 32 obligate heterozygotes (16 males and 16 females) for this disease and 20 controls (10 males and 10 females). After collection, the cells were transported in dry ice to the laboratory, where they were assayed. The assays were repeated after the cells had been stored for 12 months. beta-Glucosidase activity was assayed with D-[glucose-U-14C]glucosylceramide at pH 5.8 with Cutscum-Na-cholate as a detergent and 4-methylumbelliferyl-beta-glucoside at pH 4.1 with Triton-Na-taurocholate as a detergent. The activities of two marker enzymes, 4-methylumbelliferyl-beta-galactosidase and N-acetyl-beta-glucosaminidase, were assayed in aliquots of the same leukocyte samples. The activity of beta-galactosidase remained constant during storage, N-acetyl-beta-glucosaminidase increased, while beta-glucosidase decreased as assayed with the natural as well as with the artificial substrate. beta-Glucosidase activity was significantly lower in the female than in male controls and heterozygotes. When assayed with natural substrate beta-glucosidase activity in leukocytes from the male patients was 6--12% of the control mean value and 10--15% in those from the female patients. The corresponding figures found when the artificial substrate was used were 15--30% and 22--45%. The values for the heterozygotes were respectively 42--68% and 34--79% with the natural substrate, and 33--82% and 51--109% with the artificial substrate. No correlation was found between the age of the patient and the beta-glucosidase activity.

Acetylglucosamine↗
PubMed1984

Uptake and stability of human and bovine acid alpha-glucosidase in cultured fibroblasts and skeletal muscle cells from glycogenosis type II patients.

Acid alpha-glucosidase (EC 3.2.1.20) was purified from human placenta and bovine testis by affinity chromatography using concanavalin A (conA) and Sephadex G 200. When added to the culture medium of human fibroblasts, the enzyme purified from bovine testis is taken up with a 200-fold higher efficiency than the enzyme from human placenta. Uptake of acid alpha-glucosidase from bovine testis is mediated by the mannose-6-phosphate receptor, whereas only a minor fraction of placental enzyme appears to be equipped with the mannose-6-phosphate recognition marker. Once internalized, both human and bovine acid alpha-glucosidase demonstrate a half-life of about 10 days in fibroblasts from control individuals and patients with different clinical forms of glycogenosis type II (Pompe's disease, acid alpha-glucosidase deficiency). Evidence is presented that the mannose-6-phosphate receptor is also present on the plasma membrane of the clonal myogenic skeletal muscle cell lines G8-1 and L6J1 (respectively from mouse and rat origin) and on cultured human skeletal muscle cells derived from a muscle biopsy. Addition of bovine testis acid alpha-glucosidase to skeletal muscle cell cultures from an adult patient with glycogenosis type II leads to complete correction of the enzyme deficiency.

Animals↗
PubMed1989

In vitro detergent activation of lysosomal acid beta-glucosidase in the spleen of normal and type 1 Gaucher patients is not accompanied by change in aggregation state.

The genetic defect in Gaucher disease consists in a deficiency of a membrane-bound lysosomal acid beta-glucosidase. Using the radiation inactivation method, we have previously reported a subunit coupling of the mutated acid beta-glucosidase from Gaucher type 1 spleen in contrast to the normal one (Maret, A., Potier, M., Salvayre, R. and Douste-Blazy, L. (1983) FEBS Lett. 160, 93-97). We have used the same method to determine the effect of detergents on subunit coupling or uncoupling of acid beta-glucosidase in normal and Gaucher spleens. The hypothesis that detergent activation of beta-glucosidase could be due to subunit association or dissociation has been tested. The radiation inactivation size of beta-glucosidase in absence of detergent was 71,000 and 135,500 for normal and Gaucher spleen, respectively, whereas the corresponding values in presence of detergent were 84,000 and 169,000. The higher values obtained in the presence of detergent are incompatible with association or dissociation of subunits but correspond to the increase generally observed for proteins irradiated in the presence of Triton X-100.

Detergents↗