Dr. Betty M Tam MD
Internist
1133 East Stanley Blvd # 101 Livermore CA, 94550About
Dr. Betty Tam is an internist practicing in Livermore, CA. Dr. Tam specializes in the medical treatment of adults. Internists can act as a primary physician or a consultant to a primary physician. They manage both common and rare diseases. Dr. Tam provides comprehensive care and manages treatment with surgeons as well. Internists establish long-term relationships with their patients and incorporate disease prevention and mental health care into their practice.
Education and Training
St George',s University MD
St George',s University 2001
Board Certification
Internal MedicineAmerican Board of Internal MedicineABIM
Provider Details
Expert Publications
Data provided by the National Library of Medicine- X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
- Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: iron-release trigger and anion-binding site.
- [13C]Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride.
- Fluorescent photoreceptors of transgenic Xenopus laevis imaged in vivo by two microscopy techniques.
- Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe.
- Identification of an outer segment targeting signal in the COOH terminus of rhodopsin using transgenic Xenopus laevis.
- Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe.
- Mutant rab8 Impairs docking and fusion of rhodopsin-bearing post-Golgi membranes and causes cell death of transgenic Xenopus rods.
- On-line monitoring and control of methanol concentration in shake-flask cultures of Pichia pastoris.
- Production and isolation of the recombinant N-lobe of human serum transferrin from the methylotrophic yeast Pichia pastoris.
- Association of the two lobes of ovotransferrin is a prerequisite for receptor recognition. Studies with recombinant ovotransferrins.
- Effects of mutations of aspartic acid 63 on the metal-binding properties of the recombinant N-lobe of human serum transferrin.
- Receptor recognition sites reside in both lobes of human serum transferrin.
- Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase.
- Inequivalence of the two tyrosine ligands in the N-lobe of human serum
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