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Biomedical subjects

J C May

Publications and source records attributed to J C May.

At least 19 recordsLinked to original sources
PubMed2000

The determination of phosphorus in Haemophilus influenzae type b conjugate vaccines by inductively coupled plasma-atomic emission spectrometry.

This study describes a method for the determination of phosphorus in lyophilized Haemophilus influenzae type b conjugate vaccines by inductively coupled plasma-atomic emission spectroscopy (ICP-AES). The concentration of polysaccharide is directly related to the concentration of phosphorus as measured in the laboratory. Phosphorus is present in the polyribosyl-ribitol phosphate (PRP) group of the Haemophilus influenzae type b conjugate vaccine. The repeating unit of PRP is 3-B-D ribose[1-1]ribitol-5-phosphate. Phosphorus in the final container is measured in microg per dose. The amount of PRP is calculated from this and reported in microg per dose. The Haemophilus influenzae type b conjugate vaccine was analyzed for phosphorus content within the range of 1.34 to 2.02 microg phosphorus per ml. The relative difference of phosphorus concentrations determined by the ICP-AES method from the phosphorus concentrations determined by the traditional colorimetric molybdate method ranged from 2.2 to 10.6%. Phosphorus spike recovery for the vaccine ranged from 93 to 99% (1.93+/-0.13 microg P/ml). The phosphorus determination of NIST SRM 3139 phosphorus spectrometric solution differed by 3.0% from the certified phosphorus value (10.00 mg P/ml).

Bacterial Capsules↗
PubMed1997

Length polymorphism within the second variable region of the human immunodeficiency virus type 1 envelope glycoprotein affects accessibility of the receptor binding site.

Sequential mutations were introduced into the V2 region of human immunodeficiency virus (HIV) type 1 HXB2, affecting the length, charge, and number of potential glycosylation sites. The insertions had no effect on cytopathicity or on the ability of virus to replicate in peripheral blood mononuclear cells and established T-cell lines. However, deletion of amino acids 186 to 188, encoding a conserved glycosylation site, resulted in a nonviable virus, suggesting a minimal length requirement of 40 amino acids for a functional V2 loop. However, all amino acid insertions affected the sensitivity of the variants to neutralization by soluble CD4 and monoclonal antibodies specific for epitopes in the V3 and CD4 binding site regions. Furthermore, these mutant viruses showed resistance to neutralization by HIV-positive human sera. Soluble gp120 mutant glycoproteins showed increased affinities for soluble CD4 and monoclonal antibodies specific for a number of epitopes overlapping the CD4 binding site, confirming that length increases in V2 affect exposure of the CD4 binding site. In summary, these data demonstrate that differences in V2 length modulate immunoreactivity of the envelope glycoprotein and support an association between the V2 and CD4 binding site regions.

Binding Sites↗
PubMed1996

Functional characterization of the V1V2 region of human immunodeficiency virus type 1.

The level of proviral DNA sequence variation in the V1V2 region was monitored over time in six HIV-1-infected individuals. Substitutional and length variation was observed, where the majority of length changes, ranging from 28 to 49 amino acids, was located within the V1 region. Evidence for convergent evolution in the V2 region was found. The functional significance of this variation was assessed by cloning the V1V2 sequences into an infectious molecular clone, HXB2. The majority of chimeras replicated, demonstrating that the sequences, though genetically distinct, were capable of conferring a viable phenotype. Chimeras expressing closely related sequences in a constant genetic background displayed different biological phenotypes, with respect to both cytopathicity and cell tropism. However, no association between primary V1V2 amino acid sequence and viability or cytopathicity of the chimeric virus was observed, suggesting that predictions of virus phenotype based on sequences alone may be incorrect. The effect of V1V2 variation on the overall gp 120 conformation was measured by expressing the gp 20 from a number of viable and nonviable clones. No differences were observed, suggesting that misfolding of the chimeric gp 120 protein was not an explanation for the nonviability of some virus clones. Several chimeras were noncytopathic and only able to replicate in PBMC cultures, demonstrating that the V1V2 region, independent of the V3 sequence, is capable of defining both tropism and cytopathicity.

Amino Acid Sequence↗
PubMed1996

Preparation of an intra-laboratory reference material--determination of the aluminum content of a pooled 5% albumin (human) solution by ETAAS, MFS and ICP-AES.

Human albumin solutions as well as other biological products intended for human use may contain aluminum as a result of intentional addition due to manufacturing protocol or through inadvertent contamination occurring during the manufacturing process. Because of the implication of aluminum in human disease, it is desirable that aluminum levels in these products be monitored. To satisfy the need for a reference material that is representative of albumin products that are intended for therapeutic use, a pooled 5% human albumin solution was prepared in bulk to serve as a reference for aluminum during analytical procedures. Aliquots of the albumin pool were analyzed for their aluminum content by three independent analytical methods, namely, electrothermal atomic absorption, molecular fluorescence and inductively coupled plasma-atomic emission spectrometry. Measured values for aluminum in the albumin solution showed good agreement between the different analytical methods. The concentration of aluminum was determined to be 0.512 microgram Al/ml by the atomic absorption method, 0.502 microgram Al/ml by molecular fluorescence, and 0.498 microgram Al/ml by the inductively coupled plasma-atomic emission method. The overall average concentration was calculated to be 0.507 microgram/ml +/- 0.009 micrograms Al/ml. The preparation of the albumin reference and its subsequent aluminum analysis is described.

Aluminum↗
PubMed1992

Aluminum content of source plasma and sodium citrate anticoagulant.

The concentration of aluminum was determined in samples of source plasma collected by the normal plasmapheresis procedure, which involves collection in anticoagulant and immediate freezing. Samples of sodium citrate anticoagulant used in the collection of source plasma were also tested for aluminum, as were empty source plasma containers and 0.9% sodium chloride infusion (USP). Samples of source plasma were collected from a geographic cross-section of the donor population in the USA by three different manufacturers. Aliquots of these samples were mixed with Triton X-100 and sulfuric acid and analyzed for aluminum by atomic absorption spectrometry using electrothermal atomization (graphite furnace) and Zeeman background correction. The arithmetic mean and standard deviation for the aluminum content of 28 samples of source plasma were found to be 25.5 +/- 8.4 ng Al/ml. The aluminum content of the individual samples of source plasma ranged from 12 to 48 ng Al/ml. The aluminum content of 6 samples from two manufacturers of the sodium citrate anticoagulant that is used in source plasma ranged from 410 to 2,080 ng/ml. Aluminum levels found in saline for infusion and nitric acid leachates from empty source plasma containers were less than 6.9 ng/ml. The level of aluminum expected in uncontaminated human blood has been estimated to be 10 ng Al/ml or less. Comparison of this figure with the present data indicates that the sodium citrate anticoagulant contributes significantly to the aluminum load of source plasma and, therefore, to the aluminum content of products such as albumin derived from source plasma.

Aluminum↗
PubMed1992

Measurement of final container residual moisture in freeze-dried biological products.

The Center for Biologics Evaluation and Research has changed its regulations pertaining to residual moisture in freeze-dried biological products as published in Title 21 of the Code of Federal Regulations for Food and Drugs. The new regulation requires that each lot of dried product be tested for residual moisture and meet and not exceed established limits as specified by an approved method on file in the product license application. The gravimetric or loss-on-drying method is no longer listed as the required method; the 1.0% moisture limit is no longer specifically stated in the regulation. These revisions were made to bring the regulation into line with changes in residual moisture testing methods and the results obtained when new testing methods were applied to the determination of residual moisture. This is illustrated with data for Measles Virus Vaccine Live and Haemophilus b Polysaccharide Vaccine using final container residual moisture test results obtained by the gravimetric, coulometric Karl Fischer, thermogravimetric and thermogravimetric/mass spectrometric methods. Guidelines for the determination of residual moisture in dried biological products have been issued to describe residual moisture test methods and procedures used to set product residual moisture limits. For most products levels of residual moisture should be low, usually from less than 1.0% to 3.0%, so that the viability, immunologic potency and therefore the stability of the product is not compromised over time.

Biological Products↗
PubMed1989

The gravimetric method for the determination of residual moisture in freeze-dried biological products.

The gravimetric test for the determination of residual moisture in freeze-dried biological products performed in a humidity- and temperature-controlled room with the use of scrupulous gravimetric analytical technique can be used to accurately determine residual moisture in freeze-dried biological products such as antihemophilic factor (human) or honey bee venom allergenic extract. This method determines the first water of hydration of sodium tartrate dihydrate (7.93%) to within 1.3% of the calculated value with a relative standard deviation of 0.3% for 10 replicates. For this gravimetric procedure, freeze-dried samples containing from 1.12 to 4.4% residual moisture had relative standard deviations ranging from 3.6 to 9.1%. Samples containing less than 1.0% residual moisture by the gravimetric method such as intravenous immune globulin and antihemophilic factor (human) had relative standard deviations ranging from 16.7 to 47.0%. Relative standard deviations for residual moisture tests performed on comparable samples by the Karl Fischer and thermogravimetric methods showed similar variability.

Animals↗
PubMed1988

The determination of low levels of aluminum in antihemophilic factor (human) preparations by flame atomic absorption spectrometry.

Aluminum hydroxide is used to adsorb extraneous protein during the preparation of Antihemophilic Factor (Human) (AHF). Removal of Al(OH)3 is accomplished by centrifugation and filtration. This study describes a method for the determination of residual aluminum in AHF by flame atomic absorption spectrometry. Matrix interferences were minimized by employing sample digestion with HNO3 prior to nebulization in a nitrous oxide-acetylene flame. Under these conditions, the limit of detection of aluminum in an aqueous system was estimated to be approximately 0.13 micrograms Al ml-1, while the limit of quantitation was estimated to be approximately 0.56 micrograms Al ml-1. Residual aluminum levels in AHF determined by this method ranged from less than 0.20 micrograms ml-1 to 0.82 micrograms ml-1. Butyl alcohol was used to modify sample matrices after digestion to increase the sensitivity of the assay system. An increase in the aluminum absorption signal was demonstrated after the addition of butyl alcohol to an AHF digest.

Aluminum↗
PubMed1986

A survey of the concentrations of eleven metals in vaccines, allergenic extracts, toxoids, blood, blood derivatives and other biological products.

Approximately 85 samples of injectable biological products regulated by the Center for Drugs and Biologics of the United States Food and Drug Administration were surveyed for the presence of 11 elements, namely aluminum, arsenic, barium, cadmium, chromium, lead, mercury, selenium, thallium and zinc, by flame and flameless methods of atomic absorption spectrometry and flame emission spectrometry. The range of products tested included whole blood, red cells, plasma, normal serum albumin, antihemophilic factor, and other products derived from blood; allergenic extracts including honey bee venom and house dust allergenic extracts; vaccines such as measles virus vaccine and typhoid vaccine; and tetanus toxoid. The metal concentrations found in the majority of these products were low or undetectable. The metal levels varied from manufacturer to manufacturer, product and lot-to-lot of the same manufacturer's products. House dust allergenic extracts had the highest concentrations of arsenic (2.4 ppm), cadmium (0.28 ppm), chromium (0.6 ppm) and lead (1.5 ppm) found in the study. A high zinc concentration (24 ppm) in an immune serum globulin was attributed to the zinc-containing rubber stopper in contact with the product. A range of 0.36-3.30 ppm aluminum was found for seven 25% normal serum albumin samples from seven manufacturers. Values of 8.2, 17 and 18 ppm aluminum were found in one manufacturer's 25% normal serum albumin. These aluminum values appeared to be the result of an anomaly in this manufacturer's production that has not been repeated to date.

Allergens↗
PubMed1985

Compound odontoma in a dog.

A compound odontoma was diagnosed in the mandible of a 6-month-old dog. Histologically the tumor consisted primarily of mesenchymal tissue resembling dental pulp, odontoblasts, and areas of dentin. Smaller numbers of ameloblasts were associated with minimal enamel production. Odontomas are benign odontogenic tumors which must be differentiated from malignant bone tumors such as ameloblastic odontoma and ameloblastoma.

Animals↗
PubMed1984

The aluminum content of biological products containing aluminum adjuvants: determination by atomic absorption spectrometry.

Aluminum compounds are used as adjuvants in certain types of vaccines, toxoids and allergenic extracts for human use. The most common Al compounds used in biological products to enhance the immune response are aluminum potassium sulphate (alum), aluminum hydroxide and aluminum phosphate. This study describes an atomic absorption spectrometric method for the determination of the Al content of Al adsorbed toxoid preparations and allergenic extracts at levels of less than 0.85 mg of Al per half millilitre human dose. Aliquots of the samples which contained Al suspensions were acid digested with nitric and sulphuric acid and analysed in the nitrous oxide-acetylene flame of an atomic absorption spectrometer. The 396.2 nm Al line was used for analysis. The Al content of the National Bureau of Standards (NBS) Standard Reference Material No. 1075a aluminum 2- ethylhexanoate was determined to within 1% of the NBS certificate value by this method. Atomic absorption results for the Al content of tetanus toxoids containing aluminum potassium sulphate and aluminum phosphate were compared with polarographic and inductively coupled argon plasma (ICP) emission spectrometry results. Reproducibility and recovery data for Al are tabulated for a variety of biological products containing aluminum phosphate, aluminum potassium sulphate and aluminum hydroxide adjuvants. In addition, ICP has been used to characterize the Al and P compositions of the precipitates and supernatant solutions which resulted from centrifuging toxoid suspensions that contained the three different Al adjuvants.

Adjuvants, Immunologic↗
PubMed1981

Protein nitrogen unit precipitation procedure for allergenic extracts: collaborative study.

Protein nitrogen unit (NU) determination is one of the methods used to test and label the concentration of allergenic extracts. This recently standardized method is applicable to all allergenic extracts. One PNU/mL is equivalent to 1 X 10(-5) mg nitrogen determined to be in the material precipitated from 1 mL allergenic extract by phosphotungstic acid (PTA), a protein precipitant. The nitrogen is quantitated by the Kjeldahl method or another analytical method of equivalent accuracy and precision. A collaborative study of the optimized PNU precipitation method in which 6 samples were analyzed in duplicate by 6 laboratories using the Kjeldahl method for the determination of nitrogen yielded a mean of 0.1358 mg N/mL, a repeatability standard deviation and coefficient of variation of 0.0071 mg N/mL and 5.23%, respectively, and a reproducibility standard deviation and coefficient of variation of 0.0188 mg N/mL and 13.84%, respectively. The method has been adopted official first action.

Allergens↗
PubMed1979

Allergenic and biologic activity of commercial preparations of house dust extract.

The endotoxin, protein nitrogen unit (PNU) content, and allergenic activity of seven different extracts of house dust were determined. The PNU content varied from 1,600 to 44,000 PNU/ml. The endotoxin content as measured by the limulus assay varied from 450 to 500,000 ng/ml. Pyrogenic activity was present by rabbit fever assay and correlated well with the limulus assay. There was no correlation between endotoxin and PNU content of the different dust preparations. Leukocytes from 15 patients with a clinical history of allergy to dust were used for histamine release studies. The allergenic activity did not correlate with the PNU or endotoxin content of the different house dust preparations. The dust extracts could be divided into three groups according to their activities: three extracts which were the most reactive (30% histamine release with 0.12 to 0.39 PNU/ml), two which were about 20 times less active (4.75 to 6.43 PNU/ml for 30% histamine release), and a final group of two which were about 600 times less active. The leukocytes of three out of 15 patients failed to release histamine with one of these least reactive extracts. The reactivity pattern of five of the dust preparations appeared to correlate, suggesting that the different preparations contained the same allergens. Reactivities of two of the other extracts correlated poorly, and the reactivity of the least reactive sample did not correlate with six out of the seven preparations. Therefore, some dust preparations contain significant endotoxin-like material. Wide variations in the endotoxin, PNU content, allergenic activity, and reactivity patterns of different dust preparations were observed.

Adult↗
PubMed1979

Optimization of parameters in protein nitrogen unit precipitation procedure for allergenic extracts.

This work establishes the optimum conditions for the protein nitrogen unit (PNU) phosphotungstic acid (PTA) precipitation procedure for allergenic extracts. The volume of extract analyzed, the dilution of the extract prior to precipitation, the percent PTA in the precipitating solution, the washing of the precipitate, and the volume of concentrated HCl initially added to the extract were optimized, as they were found to be the factors which affected the amount of PTA precipitate obtained. Varying the digestion time, the digestion temperature, and the percent HCl in the 15% PTA precipitating solution did not cause detectable differences in the PNU values of the extracts studied.

Allergens↗
PubMed1979

Spontaneous zinc deficiency in marmosets, saguinus mystax.

Moustached marmosets, Saguinus mystax, developed alopecia, skin lesions and general debilitation approximately 6 months after being brought into our laboratory. These lesions resembled the signs of zinc deficiency in pigs, rats and squirrel monkeys. The marmosets were fed a commercial monkey diet containing 150 parts per million zinc and about 100 g of apples and oranges per week. The addition of 40 parts per million zinc to the drinking water brought about improvement in hair coat and skin condition.

Administration, Oral↗