The esophageal bird’s beak sign

Abdominal Radiology -     

Purified Roswell Park cultured antilymphocytic globulin RPMI-CALG: preparation and clinical trial

Purified human antilymphocytic globulin (RPMI-CALG) has been prepared in bulk quantities by immunization of horses with purified normal lymphocytes maintained in continuous cell culture at the Roswell Park Cell Plant. The characterization studies herein described reveal RPMI-CALG to be purified, nontoxic, and nonpyrogenic with specific in vitro immunosuppressive activity. Contamination with hemolysins and hemagglutinins is minimal and in marked contrast to other available preparations. Initial clinical trials with a lyophilized preparation reveal that it can be safely administered intravenously to humans without untoward effects. Comparison of hematological data was made on patients receiving RPMI-CALG pretransplant without other immunosuppressive agents to the same patients post-transplant receiving RPMI-CALG plus azathioprine and prednisone. No significant depressive hematological effect was apparent. Platelets were not depressed. Eosinophilia was not seen acutely or on follow-up examination. Urticaria was not evident. Follow-up studies up to 6 months after allografting failed to reveal any specific toxicity in the measured hematological parameters. This purified preparation merits further clinical trial.     

Monitoring human immunodeficiency virus type 1-infected patients by ratio of antibodies to gp41 and p24

Antibody responses of 85 patients to human immunodeficiency virus type 1 antigens were quantitated by densitometric analysis of Western blot (immunoblot) assays. All patients had been classified into the following three clinical categories: asymptomatic (ASY), acquired immunodeficiency syndrome (AIDS)-related complex (ARC), or AIDS. Fifty of the patients were monitored for 6 to 29 months. The gp41/p24 antibody ratio was examined in three studies. In the first study, initial specimens from each patient were analyzed. The mean gp41/p24 antibody ratios were 1.5 (ASY), 3.2 (ARC), and 5.4 (AIDS). Of ASY patients, 79% had antibody ratios of less than 2.0. In contrast, 72% of patients with AIDS had ratios of greater than or equal to 2.0. In the second study, serially obtained specimens from ASY, ARC, and AIDS patients were analyzed. These patients were further grouped according to progression of their clinical condition. Of ASY patients whose clinical condition progressed to ARC, 80% consistently had ratios of greater than or equal to 2.0. Of ARC patients whose clinical condition progressed to AIDS, 71% consistently had ratios of greater than or equal to 2.0. Of AIDS patients who died during the study, 100% consistently had ratios of greater than or equal to 2.0. No patients were treated with azidothymidine during the first two studies. In the third study, AIDS patients were monitored before and during treatment with azidothymidine. During treatment, ratios stabilized or improved transiently in five of seven patients. In these three studies, a gp41/p24 antibody ratio of less than 2.0 correlated with a benign clinical state and a ratio of greater than or equal to 2.0 correlated with AIDS or progression to AIDS.     

Conversion of MM creatine kinase isoforms in human plasma by carboxypeptidase N

This study was undertaken to identify the carboxypeptidase(s) (CPase) in plasma mediating sequential conversion of the tissue isoform of the MM isoenzyme of creatine kinase (MM3 CK) to MM2 and MM1 isoforms and to elucidate relationships between CPase activity measured in plasma and observed rates of isoform conversion in vitro. Purified MM3 was incubated at 37 degrees C in plasma from normal subjects and patients with acute myocardial infarction. Isoforms were quantified by chromatofocusing. Preincubation with antiserum to CPase N prevented conversion of added MM3 to MM2 and MM1. Isoform conversion rates in the absence of antibody were proportional to plasma CPase N activity assayed spectrophotometrically by hydrolysis of furylacryloyl-L-alanyl-L-lysine substrate (r = 0.89, n = 8). Plasma CPase N activity varied by nearly 300% among individuals, but average activity was similar in samples from normal subjects (267 +/- 45 [SD] U/L, n = 18), those from outpatients with angina (289 +/- 43 U/L, n = 9), and those obtained at hospital admission from patients with acute infarction (Q wave: 279 +/- 70 U/L, n = 16; non-Q wave: 272 +/- 61 U/L, n = 14) or unstable angina (280 +/- 71 U/L, n = 11). In patients with Q wave infarction, CPase N activity increased by 43% +/- 25% between 48 hours and 72 hours (P less than 0.005 compared with admission) with a concomitant change in the rate of conversion of isoforms. Thus, the rate of conversion of isoforms in individual subjects can be estimated by assay of CPase N activity in plasma.(ABSTRACT TRUNCATED AT 250 WORDS)     

Properties of fragments of human Wassermann antibodies

γG-globulins† from human syphilitic sera when treated with pepsin are still capable of flocculating cardiolipin antigen but lose their ability to fix guinea-pig complement in the presence of antigen.     

Densitometric analysis of Western blot (immunoblot) assays for human immunodeficiency virus antibodies and correlation with clinical status.

Western blot assays for antibodies directed against components of human immunodeficiency virus (HIV) associated with acquired immunodeficiency syndrome (AIDS) were examined with a densitometer and integrator. Antibody responses to seven HIV proteins were determined from the areas under the peaks of bands on blots from 430 seropositive individuals. Antibody responses corresponded qualitatively and quantitatively with clinical status. The Western blot assays examined were done on single specimens from individuals in one of four clinical states: asymptomatic with no risk factor identified, asymptomatic with risk factor(s) identified, AIDS-related complex, and AIDS. The ratios of gp41 antibody to p24 antibody and of gp41 antibody to total HIV antibodies increased, and the number of total HIV antibodies decreased progressively in these populations. Parameters were assigned to characterize the typical response found in AIDS: gp41 antibody/p24 antibody ratio, greater than or equal to 2.0; gp41 antibody/total HIV antibodies ratio, greater than or equal to 0.30; and number of total HIV antibodies, less than or equal to 25.0 signal units. Parameter match increased with progression of clinical status. These parameters were applied in a brief follow-up study of 34 HIV-infected asymptomatic individuals who developed AIDS-related complex or AIDS. Initial specimens showed a stronger correlation than our population data base had predicted, suggesting that the parameters have prognostic value. Densitometric analysis of antibody responses on Western blot assays of single or serial specimens should prove useful to physicians in staging and monitoring HIV-infected individuals and in predicting which individuals will progress to AIDS.     

Effect of zinc on lysis of sheep erythrocytes by guinea pig C4-deficient serum

The divalent cation Zn²⁺ enhanced the lysis of sheep erythrocytes (ShE) by guinea pig C4-deficient (C4D) serum. Enhancement by Zn²⁺ (0.1 mM) was demonstrated in the presence of cobra venom factor (CoVF, 2 units/ml) and optimal Mg²⁺ (1.0 mM). Moreover, Zn²⁺ (0.1 mM) in the presence of Mg²⁺ (1.0 mM) caused the lysis of ShE by C4D serum without the addition of CoVF. Further studies were therefore performed in the absence of CoVF. Although addition of Zn²⁺ or Mg²⁺ alone to some pools of C4D serum caused lysis of ShE, the greatest extent of lysis occurred when Zn²⁺ and Mg²⁺ were both added to the reaction mixtures. When C4D serum was resin-treated, both Mg²⁺ and Zn²⁺ were required for lysis. Addition of Ca²⁺ had no effect. This pathway required high concns of serum and was inhibited by pretreating the serum with zymosan (2 mg/ml serum, 37°C, 1 hr) or by heating the serum at 56°C for 20 min. K76-COOH monocarboxylic acid also inhibited this pathway. These results suggest that Zn²⁺ together with Mg²⁺ activates the alternative pathway on the nonactivator surface (ShE).