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At least 19 recordsLinked to original sources
PubMed1975

The isolation and characterisation of a platelet-specific beta-globulin (beta-thromboglobulin) and the detection of antiurokinase and antiplasmin released from thrombin-aggregated washed human platelets.

A protein fraction was isolated from the supernatant of thrombin-aggregated washed human platelets and was shown, by immunodiffusion techniques, to contain a platelet-specific beta-globulin (beta-thromboglobulin) as the major component. A molecular weight of 35 800 was determined for beta-thromboglobin from the measured sedimentation coefficient of3.0 S and Stokes radius of 2.85 nm. Beta-Thromboglobin was detected in the serum from whole blood and the supernatant of 48-h-old platelet-rich plasma and 28-day-old citrated whole blood, but not in platelet-poor plasma. The fraction containing beta-thromboglobulin was shown to possess an antiurokinase activity but was devoid of antiplasmin activity. A further fraction of approximate molecular weight 70 000 was also isolated which contained an antiplasmin but was devoid of antiurokinase activity.

Animals↗
PubMedDate not supplied

[Immuno-chemical and physico-chemical properties of human prostatic beta-globulin].

Distribution of prostate beta-globulin in tissues was studied by means of rocket-linear immunoelectrophoresis. The concentration of protein, exceeding 0.1 microgram/ml, was detected only in prostate extracts, seminal plasma and prostatic fluid. Purification of human prostate beta-globulin and its main physico-chemical properties are described. The charge of the protein molecule was altered under influence of various factors. A minor carbohydrate component was detected in the prostate beta-globulin; the protein was found to interact noncovalently with heteropolysaccharides (heparin, dextran sulfate).

Beta-Globulins↗
PubMed1980

[On the origin and diagnostic value of the CSF-beta-globulins (author's transl)].

208 cerebrospinal fluid samples were taken from patients having various patterns of neurological diseases. The following beta-globulins: transferrin, haemopexin, beta-1 A-globulin, beta-1 E-globulin, beta-2-glycoproteid and beta-lipoproteid were determined immunologically quantitatively in the CSF and partly quantitatively in the serum, and their behaviour was compared with that of the beta and tau fraction in CSF electrophoresis. It was found that changes in the fractions in CSF electrophoresis agreed only slightly with those of the quantitatively determined globulins, although these globulins represent 70--80% of the beta and tau fraction. Increases in the number of beta-1 A and beta-1 E-globulins are more significantly marked in intracranial haemorrhages than with other diseases. In all other respects, increases or decreases in the number of beta-globulins do not appear to be typical of any particular disease pattern determined by electrophoresis or quantitatively. Due to the linearity of the changes in case of disturbances of the CSF barrier, and also on account of the absolutely parallel behaviour of the beta-globulins, it was concluded that transferrin--contrary to the opinion held so far--is produced cerebrally in only small quantities or possibly not at all, and that the entirety of beta-globulins originate from the serum.

Adolescent↗
PubMed1976

[Obtaining the beta-globulin fractions from swine and cattle sera and a study of their immunological activity].

The rivanol precipitation was used to obtain beta-globulin fractions from specific swine sera against edema disease, paratyph and Aujeszky's disease as well as from normal ovine and swine sera. Agar electrophoresis revealed that the preparations produced contained beta-globulin (86 per cent), gamma-globulin (5 per cent), and alpha2-globulin (9 per cent). The beta-globulin preparations were studied for the presence of antibodies against E. coli, Salmonellae, staphylococci, myxovirus parainfluenza-3, adenoviruses, and the virus of Aujeszky's disease. The beta-globulin fraction of the specific serum against edema disease was shown to contain OK and O agglutinizing antibodies against E. coli, having a titer of up to 1:3200, and the gamma-globulin titers of up to 1:12800. The beta-globulin fraction of the specific serum against typhoid contained OH and O agglutinizing antibodies against Salmonella cholerae suis with a titer of up to 1:2560. The agglutinizing antibodies against staphylococci were twice as much in the beta-globulin fraction as compared with those in the gamma-globulin fraction. The antibodies against Aujeszky's disease and the adenoviruses in the beta-globulin fractions were in negligible amounts, and the titer of the antibodies against myxovirus parainfluenza-3 ranged from 1:128 to 1:512.

Adenoviridae↗
PubMed1983

[Trophoblastic beta-globulin in immunoglobulin preparations].

The content of trophoblastic beta-globulin in 142 lots of commercial immunoglobulin preparations from 20 manufacturers, produced from placental, abortion and donor blood sera, has been studied. 83% of lots from abortion blood serum and 94% of lots from placental blood serum have been found to contain the admixture of this beta-globulin, its concentration in the lots from placental blood serum being significantly higher. The method for the detection of trophoblastic beta-globulin may be used for evaluating the quality of immunoglobulin preparations as it indicates the degree of their purification from placental proteins.

Abortion, Spontaneous↗
PubMed1988

Nucleotide sequence of cloned cDNA coding for pumpkin 11-S globulin beta subunit.

cDNA coding for preproglobulin beta, a precursor protein of 11-S globulin beta subunit, was cloned and the nucleotide sequence has been determined. The sequence covers the whole coding region (1440 base pairs) with 5' and 3' noncoding region (30 and 214 base pairs, respectively). The deduced amino acid sequence of preproglobulin beta consists of a 21-amino-acid N-terminal signal peptide, preceding the acidic gamma polypeptide region (275 amino acids) and the subsequent basic delta region (184 amino acids). The site for post-translational cleavage of the precursor polypeptide to make the gamma and delta chains is estimated to be located between the asparagine-glycine residues. The N-terminal amino acid of the gamma chain of mature 11-S globulin beta subunit was reported to be blocked by 5-oxoproline (pyroglutamic acid) [Ohmiya et al. (1980) Plant Cell Physiol. 21, 157-167]. It was shown that the blocked N-terminal amino acid is coded as a glutamine residue. The derived amino acid sequence was also compared with those of precursor proteins of other 11-S globulins such as soybean glycinin, cotton beta globulin, pea legumin and rape 11-S globulin by dot matrix analysis.

Amino Acid Sequence↗
PubMed2002

[Diagnosis of bacterial pneumonia by serum beta-globulin demarcation].

We studied whether the consolidation whose serum beta-globulin demarcation showed more than 12% was bacterial pneumonia or not. The materials were the patients with fever (> or = 37 degrees C) and the consolidation on chest-X ray film, the value of serum beta-globulin demarcation was more than 12% from 1995 to 2000. There were 5 cases with drug-induced pneumonitis, 5 cases with BOOP, 2 cases with eosinophilic pneumonia, 1 case with lung cancer (adenocarcinoma), and 1 case with interstitial pneumonia with dermatomyositis. No one had bacterial pneumonia. These results suggested the consolidation with fever whose serum beta-globulin demarcation showed more than 12% was not bacterial pneumonia.

Aged↗
PubMed1981

Polyclonal gammopathy with beta-globulin-gamma-globulin bridging. Two unusual cases.

Polyclonal gammopathy with beta-globulin-gamma-globulin (beta-gamma) bridging has been classically, though not exclusively, described with cirrhosis. We studied two unusual cases that exhibited polyclonal gammopathy with beta-gamma bridging. In the first case, the coexistence of Kaposi's sarcoma appeared with angioimmunoblastic lymphadenopathy. In the second, liver disease developed as a complication of alpha 1-antitrypsin deficiency and retroperitoneal malignant fibrous histiocytoma involving the porta hepatis.

Aged↗
PubMed1992

[Cellular localization of human secretory beta globulin in normal and tumor tissues].

Distribution of secretory beta-globulin (S beta G) which possesses affinity for steroids was investigated immunohistochemically. Tissue specificity of S beta G, produced in adult secretory epithelial cells of the seminal vesicles, salivary glands, prostate, bronchi and mammary gland was discovered. The protein was not detected in fetal and embryonal tissues. S beta G synthesis is abnormal in neoplasms: its expression partly preserves in breast cancer cells and increases in epithelium of mammary ducts near the focus of malignancy. In lung cancer and bronchial glands cells near the focus of neoplastic transformation S beta G positive reaction was not observed.

Adult↗
PubMed1992

Association of proteins in acidic solutions--a case study with beta-globulin.

The investigation of the effect of acid pH on the structure of beta-globulin indicated several transitions as a function of pH. Upon reducing the pH from 7.0, the beta-globulin molecule underwent an expansion due to hydration up to pH 5.0, and a further increase in H+ concentration resulted in unfolding. This is a single step cooperative denaturation as indicated by the viscosity profile. At extreme acid pH values (below pH 2.0) the protein associates or folds to a different conformational motif as shown by blue shift of ultraviolet fluorescence emission maximum and decrease in reduced viscosity values by more than 30% due to an entropically driven hydrophobic interaction. The conformational analysis of beta-globulin showed a decrease up to pH 3.0, followed by an increase in the ordered structure at low pH values indicating that the low pH values stabilized this new conformation. These results are discussed in view of the molten globule structure of proteins.

Beta-Globulins↗